43117
2009
2020
eng
225
233
11
945
postprint
1
2020-06-04
2020-06-04
--
Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer
An efficient electrocatalytic biosensor for sulfite detection was developed by co-immobilizing sulfite oxidase and cytochrome c with polyaniline sulfonic acid in a layer-by-layer assembly. QCM, UV-Vis spectroscopy and cyclic voltammetry revealed increasing loading of electrochemically active protein with the formation of multilayers. The sensor operates reagentless at low working potential. A catalytic oxidation current was detected in the presence of sulfite at the modified gold electrode, polarized at +0.1 V ( vs. Ag/AgCl 1 M KCl). The stability of the biosensor performance was characterized and optimized. A 17-bilayer electrode has a linear range between 1 and 60 mu M sulfite with a sensitivity of 2.19 mA M-1 sulfite and a response time of 2 min. The electrode retained a stable response for 3 days with a serial reproducibility of 3.8% and lost 20% of sensitivity after 5 days of operation. It is possible to store the sensor in a dry state for more than 2 months. The multilayer electrode was used for determination of sulfite in unspiked and spiked samples of red and white wine. The recovery and the specificity of the signals were evaluated for each sample.
Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
10.25932/publishup-43117
urn:nbn:de:kobv:517-opus4-431176
1866-8372
Analytical and Bioanalytical Chemistry 393 (2009) 225–233 DOI:10.1007/s00216-008-2432-y
Keine öffentliche Lizenz: Unter Urheberrechtsschutz
Roberto Spricigo
Roman Dronov
Fred Lisdat
Silke Leimkühler
Frieder W. Scheller
Ursula Wollenberger
Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
945
eng
uncontrolled
bioelectrocatalysis
eng
uncontrolled
sulfite
eng
uncontrolled
sulfite oxidase
eng
uncontrolled
cytochrome c
eng
uncontrolled
multilayer
Chemie und zugeordnete Wissenschaften
open_access
Mathematisch-Naturwissenschaftliche Fakultät
Referiert
Open Access
Universität Potsdam
https://publishup.uni-potsdam.de/files/43117/pmnr945.pdf
11958
2006
2006
eng
article
1
--
--
--
Ferroceneboronic acid-based amperometric biosensor for glycated hemoglobin
An amperometric biosensor for the determination of glycated hemoglobin in human whole blood is proposed. The principle is based on the electrochemical measurement of ferroceneboronic acid (FcBA) that has been specifically bound to the glycated N-terminus. Hemoglobin is immobilized on a zirconium dioxide nanoparticle modified pyrolytic graphite electrode (PGE) in the presence of didodecyldimethylammonium bromide (DDAB). The incubation of this sensor in FcBA solution leads to the formation of an FcBA-modified surface due to the affinity interaction between boronate and the glycated sites of the hemoglobin. The binding of FcBA results in well-defined redox peaks with an E-0' of 0.299 V versus Ag/AgCl (1 M KCl). The square wave voltammetric response of the bound FcBA reflects the amount of glycated hemoglobin at the surface. This signal increases linearily with the degree of glycated hemoglobin from 6.8 to 14.0% of total immobilized hemoglobin. The scheme was applied to the determination of the fraction of glycated hemoglobin in whole blood samples.
http://www.sciencedirect.com/science/journal/09254005
10.1016/j.snb.2005.07.011
0925-4005
allegro:1991-2014
10101341
Sensors and actuators / B. - ISSN 0925-4005. - 113 (2006), 2, S. 623 - 629
Songqin Liu
Ursula Wollenberger
Martin Katterle
Frieder W. Scheller
Institut für Biochemie und Biologie
Referiert
12278
2010
2010
eng
article
1
--
--
--
Redox properties and catalytic activity of surface-bound human sulfite oxidase studied by a combined surface enhanced resonance Raman spectroscopic and electrochemical approach
Human sulfite oxidase (hSO) was immobilised on SAM-coated silver electrodes under preservation of the native heme pocket structure of the cytochrome b5 (Cyt b5) domain and the functionality of the enzyme. The redox properties and catalytic activity of the entire enzyme were studied by surface enhanced resonance Raman (SERR) spectroscopy and cyclic voltammetry (CV) and compared to the isolated heme domain when possible. It is shown that heterogeneous electron transfer and catalytic activity of hSO sensitively depend on the local environment of the enzyme. Increasing the ionic strength of the buffer solution leads to an increase of the heterogeneous electron transfer rate from 17 s(-1) to 440 s(- 1) for hSO as determined by SERR spectroscopy. CV measurements demonstrate an increase of the apparent turnover rate for the immobilised hSO from 0.85 s(-1) in 100 mM buffer to 5.26 s(-1) in 750 mM buffer. We suggest that both effects originate from the increased mobility of the surface-bound enzyme with increasing ionic strength. In agreement with surface potential calculations we propose that at high ionic strength the enzyme is immobilised via the dimerisation domain to the SAM surface. The flexible loop region connecting the Moco and the Cyt b5 domain allows alternating contact with the Moco interaction site and the SAM surface, thereby promoting the sequential intramolecular and heterogeneous electron transfer from Moco via Cyt b5 to the electrode. At lower ionic strength, the contact time of the Cyt b5 domain with the SAM surface is longer, corresponding to a slower overall electron transfer process.
http://www.rsc.org/Publishing/Journals/CP/index.asp
10.1039/B927226g
1463-9076
allegro:1991-2014
10107773
Physical chemistry chemical physics. - ISSN 1463-9076. - 12 (2010), 28, S. 7894 - 7903
Murat Sezer
Roberto Spricigo
Tillmann Utesch
Diego Millo
Silke Leimkühler
Maria A. Mroginski
Ursula Wollenberger
Peter Hildebrandt
Inez M. Weidinger
Institut für Biochemie und Biologie
Referiert
13363
2005
2005
deu
Getr. Zählung : graph. Darst.
doctoralthesis
Potsdam
1
--
--
--
Kopplung von Biomolekülen mit Elektroden : von Bioelektrochemie zur Biosensorik
allegro:1991-2014
10101364
Ursula Wollenberger
Institut für Biochemie und Biologie
Nicht referiert
13491
2005
2005
eng
article
1
--
--
--
Cytochrome P450 biosensors : a review
Cytochrome P450 (CYP) is a large family of enzymes containing heme as the active site. Since their discovery and the elucidation of their structure, they have attracted the interest of scientist for many years, particularly due to their catalytic abilities. Since the late 1970s attempts have concentrated on the construction and development of electrochemical sensors. Although sensors based on mediated electron transfer have also been constructed, the direct electron transfer approach has attracted most of the interest. This has enabled the investigation of the electrochemical properties of the various isoforms of CYP. Furthermore, CYP utilized to construct biosensors for the determination of substrates important in environmental monitoring, pharmaceutical industry and clinical practice. (c) 2004 Elsevier B. V. All rights reserved
allegro:1991-2014
10102889
Biosensors & Bioelectronics. - 20 (2005), 12, S. 2408 - 2423
Nikitas Bistolas
Ursula Wollenberger
Christiane Jung
Frieder W. Scheller
Institut für Biochemie und Biologie
Referiert
14414
2004
2004
eng
article
1
--
--
--
Myoglobin-Clay Electrode for Nitric Oxide (NO) Detection in Solution
allegro:1991-2014
10097316
Electroanalysis. - 16 (2004), 4, S. 253 - 259
Steffen Kröning
Frieder W. Scheller
Ursula Wollenberger
Fred Lisdat
Institut für Biochemie und Biologie
Referiert
12733
2005
2005
eng
article
1
--
--
--
Application of electrically contacted enzymes for biosensors
3-527- 30690-0
allegro:1991-2014
10097374
Bioelectronics / Hrsg.: Itmar Willner ; Eugenii Katz. - Weinheim : WILEY-VCH, 2005. - 475 S. - ISBN: 3-527- 30690-0
Frieder W. Scheller
Fred Lisdat
Ursula Wollenberger
Institut für Biochemie und Biologie
Nicht referiert
13373
2005
2005
eng
article
1
--
--
--
Thirty years of haemoglobin electrochemistry
Electrochemical investigations of the blood oxygen carrier protein include both mediated and direct electron transfer. The reaction of haemoglobin (Hb) with typical mediators, e.g., ferricyanide, can be quantified by measuring the produced ferrocyanide which is equivalent to the Hb concentration. Immobilization of the mediator within the electrode body allows reagentless electrochemical measuring of Hb. On the other hand, entrapment of the protein within layers of polyclectrolytes, lipids, nanoparticles of clay or gold leads to a fast heterogeneous electron exchange of the partially denatured Hb. (c) 2005 Elsevier B.V. All rights reserved
allegro:1991-2014
10099850
Advances in Colloid and Interface Science. - 116 (2005), 1-3, S. 111 - 120
Frieder W. Scheller
Nikitas Bistolas
Songqin Liu
Michael Jänchen
Martin Katterle
Ursula Wollenberger
Institut für Biochemie und Biologie
Referiert
13757
2005
2005
eng
article
1
--
--
--
Affinity interaction betwen phenylboronic acid-carrying self-assembled monolayers and FAD or HRP
A method is provided for the recognition of glycated molecules based on their binding affinities to boronate- carrying monolayers. The affinity interaction of flavin adenine dinucleotide (FAD) and horseradish peroxidase (HRP) with phenylboronic acid monolayers on gold was investigated by using voltammetric and microgravimetric methods. Conjugates of 3-aminopherrylboronic acid and 3,3'-dithiodipropionic acid di(N-hydroxysuccinimide ester) or 11-mercaptoundecanoic acid were prepared and self-assembled on gold surfaces to generate monolayers. FAD is bound to this modified sur-face and recognized by a pair of redox peaks with a formal potential of -0.433 V in a 0.1 m phosphate buffer solution, pH 6.5. Upon addition of a sugar to the buffer, the bound FAD could be replaced, indicating that the binding is reversible. Voltammetric, mass measurements, and photometric activity assays show that the HRP can also be bound to the interface. This binding is reversible, and HRP can be replaced by sorbitol or removed in acidic solution. The effects of pH, incubation time, and concentration of H2O2 were studied by comparing the catalytic reduction of H2O2 in the presence of the electron-donor thionine. The catalytic current of the HRP-loaded electrode was proportional to HRP concentrations in the incubation solution in the range between 5 mu g mL(-1) and 0.4 mg mL(-1) with a linear slope of 3.34 mu A mL mg(-1) and a correlation coefficient of 0.9945
allegro:1991-2014
10099377
Chemistry : a European Journal. - 11 (2005), S. 4239 - 4246
Songqin Liu
Ursula Wollenberger
Jan Halamek
Eik Leupold
Walter F. M. Stöcklein
Axel Warsinke
Frieder W. Scheller
Institut für Biochemie und Biologie
Referiert
14701
2004
2004
deu
article
1
--
--
--
Elektroden-Design für elektronische Wechselwirkung mit Monooxygenasen
3-8047-2132-x
allegro:1991-2014
10097423
Metalloproteine und Metalloidproteine : analytische Aspekte, Redoxprozesse, antioxidative Schutzsysteme, Interaktion Metallle - Proteine, Pathobiochemie / Hrsg.: Antonjos Kyriakopoulos ; D. Behne. - Stuttgart : Wiss.- Verlagsges., 2004. - 166 S. - ISBN: 3-8047-2132-x
Ursula Wollenberger
Nikitas Bistolas
Christiane Jung
V. V. Shumyantseva
T. Ruzgas
Frieder W. Scheller
Institut für Biochemie und Biologie
Nicht referiert
15097
2004
2004
eng
article
1
--
--
--
Spectroelectrochemistry of cytochrome P450cam
The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4'-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4'-dithiodipyridin and dithionite modified electrodes. A formal potential (E-0') of -373 mV vs Ag/AgCl 1 M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during electrolysis. (C) 2003 Elsevier Inc. All rights reserved
allegro:1991-2014
10097314
Biochemical and Biophysical Research Communications. - 314 (2004), 3, S. 810 - 816
Nikitas Bistolas
A. Christenson
T. Ruzgas
Christiane Jung
Frieder W. Scheller
Ursula Wollenberger
Institut für Biochemie und Biologie
Referiert
15172
2004
2004
eng
article
1
--
--
--
Electrochemical parameters of phenoxazine derivatives in solution and at monolayer-modified gold electrodes
Electrochemical properties of beta-(10-phenoxazinyl) propylamine (APPX) and beta-(10-phenoxazinyl) propionic acid (PPX) have been studied in solution, and in immobilized state on gold electrodes modified with monolayers of cystamine and mercaptoundecanoic acid. A reversible diffusion-controlled process of APPX and PPX was observed at a bare gold electrode. The electrochemical conversion of both compounds at modified gold electrodes was a quasireversible diffusion-controlled process. The redox potential of immobilized APPX (443 mV) was similar to the potential in solution, while the value of the immobilized PPX was 131 mV higher than in solution. The immobilized mediators were electrocatalytically active in the fungal peroxidase-catalyzed hydrogen peroxide reduction
allegro:1991-2014
10097315
Electroanalysis. - 16 (2004), 3, S. 183 - 189
J. Kulys
K. Krikstopaitis
Frieder W. Scheller
Ursula Wollenberger
Institut für Biochemie und Biologie
Referiert
15265
2004
2004
eng
article
1
--
--
--
Characterization of self-assembling of glucose dehydrogenase in mono- and multilayers on gold electrodes
Glucose dehydrogenase (GDH) was assembled electrostatically onto QCM-gold electrodes by their sequential deposition with anionic polyelectrolytes such as PSS and PASA. For the layer-by-layer arrangements both the microgravimetric and the electrochemical sensor signal were followed. Increasing amounts of GDH were deposited by stepwise formation of alternating layers of GDH and PSS or PASA. The mass increase was about 1.88 mug/cm(2) for one GDH/ PASA bilayer and 2.4 mug/cm(2) for a GDH/PSS bilayer. The addition of phenolic compounds resulted in an oxidation current, which could be catalytically increased by the GDH catalysed reaction in the presence of glucose. The system functions as glucose sensor when quinones are present in nonlimiting amount. The amperometric response was already diffusion limited when a single layer of GDH was adsorbed. The sensor sensitivity increased by a factor of 10 when MSA was used instead of MUA as initial electrode modifier
allegro:1991-2014
10097368
Electroanalysis. - 16 (2004), 13-14, S. 1149 - 1154
Noya Loew
Frieder W. Scheller
Ursula Wollenberger
Institut für Biochemie und Biologie
Referiert
15497
2003
2003
eng
article
1
--
--
--
Enzyme acitivity of alpha-chymotrypsin after derivatization with phenolic compounds
allegro:1991-2014
10095961
Nahrung. - 47 (2003), 5, S.325 - 329
Sascha Rohn
Harshadrai Manilal Rawel
Ursula Wollenberger
Jürgen Kroll
Institut für Ernährungswissenschaft
Nicht referiert
16116
2003
2003
eng
article
1
--
--
--
An amperometric bi-enzyme sensor for determination of formate using cofactor regeneration
allegro:1991-2014
10097239
Biosensors + Bioelectronics. - 18 (2003), 9, S. 1095 - 1100
Karen K. W. Mak
Ursula Wollenberger
Frieder W. Scheller
Reinhard Renneberg
Institut für Biochemie und Biologie
Referiert
16145
2003
2003
eng
article
1
--
--
--
Enzyme Electrodes
3-527-30401-0
allegro:1991-2014
10097289
Encyclopedia of Electrochemistry : Vol. 9 Bioelectrochemistry / Hrsg.: Georg S. Wilson ; Allen J. Bard. - Weinheim : WILEY-VCH, 2002. - ISBN: 3-527-30401-0. - 662 S.
Frieder W. Scheller
Ursula Wollenberger
Institut für Biochemie und Biologie
Nicht referiert
16391
2003
2003
eng
article
1
--
--
--
Electrochemical determination of human hemoglobin by using ferrocene carboxylic acid modified carbon powder microelectrode
allegro:1991-2014
10097296
Analytical Letters. - 36 (2003), 9, S. 2049 - 2059
Jian Chen
Walter F. M. Stöcklein
Frieder W. Scheller
Ursula Wollenberger
Institut für Biochemie und Biologie
Referiert
16773
2002
2002
eng
article
1
--
--
--
Detection of escherichia coli water by culture-based amperometric and luminometric methods
allegro:1991-2014
10093445
Water science and technology. - 45 (2002), 4-5, S. 191 - 199
C. Nistor
A. Osvik
R. Davidsson
Andreas Rose
Ursula Wollenberger
Dorothea Pfeiffer
J. Emneus
L. Fiksdal
Institut für Biochemie und Biologie
16859
2002
2002
eng
article
1
--
--
--
In-field monitoring of cleaning efficiency in waste water treatment plants using two phenolsensitive biosensors
allegro:1991-2014
10093446
Analytical chemica acta. - 456 (2002), 1, S. 3 - 17
C. Nistor
Andreas Rose
M. Farre
L. Stoica
Ursula Wollenberger
T. Ruzgas
Dorothea Pfeiffer
Damia Barcelo
Lo Gorton
J. Emneus
Institut für Biochemie und Biologie
16815
2002
2002
eng
article
1
--
--
--
Electron transfer of hemoglobin at electrodes modified with colloidal clay nanoparticles
allegro:1991-2014
10093454
Analytical and bioanalytical chemistry. - 372 (2002), 2, S. 235 - 239
Chenghong Lei
Ursula Wollenberger
Nikitas Bistolas
A. Guiseppi-Eli
Frieder W. Scheller
Institut für Biochemie und Biologie
16943
2002
2002
eng
article
1
--
--
--
Bioelectrocatalysis by redox enzymes at modified electrodes
www.elsevier.nl/inca/publications/6/0/1/3/4/7/index.htt
allegro:1991-2014
10093973
Reviews in molecular biotechnology. - 82 (2002), 4, S. 411 - 424
Frieder W. Scheller
Ursula Wollenberger
Chenghong Lei
Wen Jin
Bixia Ge
Claudia Lehmann
Fred Lisdat
Vadim Fridman
Institut für Biochemie und Biologie
27737
1995
1995
eng
article
1
--
--
--
A stacked multichannel amperometric detection system
allegro:1991-2014
10082782
Micro total analysis system : proceedings of the My[Micro]TAS '94 Workshop, held at MESA Research Institute, University of Twente, Netherlands, 21.-22. Nov. 1994 / ed. by A. van Berg ; P. Bergveld. - Dordrecht [u.a.] : Kluwer, 1995. - S. 249 - 254
Manfred Paeschke
Ursula Wollenberger
A. Uhlig
Uwe Schnakenberg
B. Wagner
R. Hintsche
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
27753
1995
1995
eng
article
1
--
--
--
Properties of interdigital electrode arrays with different geometries
allegro:1991-2014
10082781
Analytica chimica acta. - 305 (1995), S. 126 - 136
Manfred Paeschke
Ursula Wollenberger
C. Köhler
T. Lisec
Uwe Schnakenberg
B. Wagner
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
35609
2012
2012
eng
33
41
9
87
article
Elsevier
Lausanne
1
--
--
--
Human sulfite oxidase electrochemistry on gold nanoparticles modified electrode
The present study reports a facile approach for sulfite biosensing, based on enhanced direct electron transfer of a human sulfite oxidase (hSO) immobilized on a gold nanoparticles modified electrode. The spherical core shell AuNPs were prepared via a new method by reduction of HAuCl4 with branched poly(ethyleneimine) in an ionic liquids resulting particles with a diameter less than 10 nm. These nanoparticles were covalently attached to a mercaptoundecanoic acid modified Au-electrode where then hSO was adsorbed and an enhanced interfacial electron transfer and electrocatalysis was achieved. UV/Vis and resonance Raman spectroscopy, in combination with direct protein voltammetry, are employed for the characterization of the system and reveal no perturbation of the structural integrity of the redox protein. The proposed biosensor exhibited a quick steady-state current response, within 2 s, a linear detection range between 0.5 and 5.4 mu M with a high sensitivity (1.85 nA mu M-1). The investigated system provides remarkable advantages in the possibility to work at low applied potential and at very high ionic strength. Therefore these properties could make the proposed system useful in the development of bioelectronic devices and its application in real samples.
Bioelectrochemistry : an international journal devoted to electrochemical aspects of biology and biological aspects of electrochemistry ; official journal of the Bioelectrochemical Society
10.1016/j.bioelechem.2011.11.012
1567-5394
wos:2011-2013
WOS:000309033000007
Frasca, S (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25,Haus 25, D-14476 Golm, Germany., uwollen@uni-potsdam.de
Cluster of Excellence "Unifying Concepts in Catalysis"; Deutsche
Forschungsgemeinschaft [EXC 314, SM 199/7-1]; ILB (TERAsens); Fonds der
Chemischen Industrie; National University of Costa Rica; National
Science Bureau of Costa Rica (MICIT); National Science Bureau of Costa
Rica (CONICIT); DAAD
Stefano Frasca
Oscar Rojas
Johannes Salewski
Bettina Neumann
Konstanze Stiba
Inez M. Weidinger
Brigitte Tiersch
Silke Leimkühler
Joachim Koetz
Ursula Wollenberger
eng
uncontrolled
Direct electron transfer
eng
uncontrolled
Gold nanoparticle
eng
uncontrolled
Human sulfite oxidase
eng
uncontrolled
Ionic liquid
eng
uncontrolled
Sulfite biosensor
Institut für Biochemie und Biologie
Referiert
335
2000
deu
176
227
bookpart
Brandenburgisches Umweltforschungszentrum
0
2005-05-24
--
--
Umweltforschung für das Land Brandenburg : Projekt Umweltanalytik / Umweltmeßtechnik / Informationssysteme
urn:nbn:de:kobv:517-opus-3862
386
Brandenburgische Umwelt-Berichte : BUB ; Schriftenreihe des Zentrums für Umweltwissenschaften der Universität Potsdam und des Brandenburgischen Umweltforschungszentrums, Neuruppin. - 8 (2000)
AR 11100
Hartmut Asche
Christine Böckmann
Steffen Laue
Hans-Gerd Löhmannsröben
Matthias Lemke
Lars Schober
Oliver Reich
Erika Lück
Marc Schütte
Horst Domsch
Alexander Makower
Frieder W. Scheller
Wolfgang Stöcklein
Ursula Wollenberger
Rainer Schultze
Theo Hengstermann
Frank Schael
Naturwissenschaften und Mathematik
open_access
Extern
Zentrum für Umweltwissenschaften
Universität Potsdam
https://publishup.uni-potsdam.de/files/335/bub8_s176-227.pdf
24741
1997
1997
eng
article
1
--
--
--
Phenol-oxidizing enzymes : mechanisms and applications
allegro:1991-2014
10088249
Frontiers in Biosensorics / Hrsg.: Frieder W. Scheller. - Basel : Birkhäuser. - Band 1: Fundamental aspects. - 1997. - (EXS ; 80). - S. 63 - 82
Martin G. Peter
Ursula Wollenberger
Institut für Chemie
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
Institut für Organische Chemie und Strukturanalytik
24743
1997
1997
eng
article
1
--
--
--
Enzymatic substrade recycling electrodes
allegro:1991-2014
10088252
Frontiers in Biosensorics / Hrsg.: Frieder W. Scheller. - Basel : Birkhäuser. - Band 2: Practical applications. - 1997. - (EXS ; 81). - S. 45 - 70
Ursula Wollenberger
Fred Lisdat
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
24731
1997
1997
eng
article
1
--
--
--
Hybrid biosensor for simultaneous electrochemical and thermal detection
allegro:1991-2014
10088216
Analytical letters. - 30 (1997), 12, S. 2141 - 2158
B. Xie
X. Tang
Ursula Wollenberger
G. Johansson
Lo Gorton
Frieder W. Scheller
B. Danielsson
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
24733
1997
1997
eng
article
1
--
--
--
Ultrasensitive bienzyme sensor for adrenaline
allegro:1991-2014
10088218
Biosensors & bioelectronics. - 12 (1997), 9/10, S, 947 - 952
Jan Szeponik
B. Möller
Dorothea Pfeiffer
Fred Lisdat
Ursula Wollenberger
Alexander Makower
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
24735
1997
1997
eng
article
1
--
--
--
Catecholamine detection using enzymatic amplification
allegro:1991-2014
10088220
Biosensors & bioelectronics. - 12 (1997), 12, S, 1199 - 1211
Alexander Markower
Ursula Wollenberger
H. Hörtnagel
Dorothea Pfeiffer
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
24736
1997
1997
eng
article
1
--
--
--
Electrochemical polymerization of functionalized thiohene derivatives for immobilization of proteins
allegro:1991-2014
10088221
Macromolecular symposia. - 126 (1997), S. 283 - 293
H.-P. Welzel
G. Kossmehl
G. Engelmann
B. Neumann
Ursula Wollenberger
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
24719
1997
1997
eng
article
1
--
--
--
Quinoprotein glucose dehydrogenase modified carbon paste electrode for detection of phenolic compounds
allegro:1991-2014
10088195
Electroanalysis. - 9 (1997), 5, S. 366 - 371
Ursula Wollenberger
B. Neumann
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
24720
1997
1997
eng
article
1
--
--
--
Electrochemistry of hemoglobin at modified silver electrodes is not a redox-process of iron protoporhyrin IX
allegro:1991-2014
10088196
Electroanalysis. - 9 (1997), 18, S. 1393 - 1396
Martin Katterle
Ursula Wollenberger
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
24723
1997
1997
eng
article
1
--
--
--
Electroanalytical determination of peroxidases and laccases on carbon paste electrodes
allegro:1991-2014
10088194
Electroanalysis. - 9 (1997), 3, S. 213 - 218
J. Kulys
A. Drungiliene
Ursula Wollenberger
K. Krikstopaitis
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
24726
1997
1997
eng
article
1
--
--
--
Electrochemical investigation of the intermolecular electron transfer between cytochrome c and NADPH-cytochrome P450-reductase
allegro:1991-2014
10088206
Journal of Electroanalytical Chemistry. - 433 (1997), 1/2, S. 135 - 139
Wen Jin
Ursula Wollenberger
E. Kärgel
W.-H. Schunck
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
26344
1996
1996
eng
article
1
--
--
--
Direct electrocatalytic determination of dissolved peroxidases
allegro:1991-2014
10082823
Analytica chimica acta. - 329 (1996), S. 231 - 237
Ursula Wollenberger
A. Drungiliene
Walter F. M. Stöcklein
J. Kulys
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
26389
1996
1996
eng
article
1
--
--
--
Enzyme/gas diffusion electrodes for determination of phenol
allegro:1991-2014
10082767
Sensors and Actuators. - 33 (1996), S. 39 - 43
A. Kaisheva
I. Iliev
R. Kazareva
S. Christov
Ursula Wollenberger
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
26390
1996
1996
eng
article
1
--
--
--
Recycling sensors based on kinases : proceedings of Mosbach Symposion on Biochemical Technology
allegro:1991-2014
10082826
Advances in Molecular and Cell Biology. - 15b (1996), S. 379 - 388
Ursula Wollenberger
Florian Schubert
Dorothea Pfeiffer
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
26395
1996
1996
eng
article
1
--
--
--
Tyrosinase-glucose dehydrogenase substrate-recycling biosensor : a highly sensitive measurement of phenolic compounds
allegro:1991-2014
10082772
Journal of Chemical Technology and Biotechnology. - 65 (1996), S. 39 - 44
Alexander Makower
A. V. Eremenko
Katrin Streffer
Ursula Wollenberger
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
31486
2010
2010
eng
article
1
--
--
--
Sulfite biosensor based on osmium redox polymer wired sulfite oxidase
A biosensor, based on a redoxactive osmium polymer and sulfite oxidase on screen-printed electrodes, is presented here as a promising method for the detection of sulfite. A catalytic oxidative current was generated when a sample containing sulfite was pumped over the carbon screen-printed electrode modified with osmium redox polymer wired sulfite oxidase. A stationary value was reached after approximately 50 s and a complete measurement lasted no more than 3 min. The electrode polarized at -0.1 V (vs. Ag vertical bar AgCl 1M KCl) permits minimizing the influence of interfering substances, since these compounds can be unspecific oxidized at higher potentials. Because of the good stability of the protein film on the electrode surface, a well functioning biosensor-flow system was possible to construct. The working stability and reproducibility were further enhanced by the addition of bovine serum albumin generating a more long-term stable and biocompatible protein environment. The optimized biosensor showed a stable signal for more than a week of operation and a coefficient of variation of 4.8% for 12 successive measurements. The lower limit of detection of the sensor was 0.5 mu M sulfite and the response was linear until 100 mu M. The high sensitivity permitted a 1:500 dilution of wine samples. The immobilization procedure and the operational conditions granted minimized interferences. Additionally, repeating the immobilization procedure to form several layers of wired SO further increased the sensitivity of such a sensor. Finally. the applicability of the developed sulfite biosensor was tested on real samples, such as white and red wines.
http://www.sciencedirect.com/science/journal/09277757
10.1016/j.colsurfa.2009.09.001
0927-7757
allegro:1991-2014
10107797
Colloids and Surfaces A - physicochemical and engineering aspects. - ISSN 0927-7757. - 354 (2010), 1-3, S. 314 - 319
Roberto Spricigo
Claudia Richter
Silke Leimkühler
Lo Gorton
Frieder W. Scheller
Ursula Wollenberger
Institut für Biochemie und Biologie
Referiert
27678
1995
1995
eng
article
1
--
--
--
Dynamic redox recycling of cytochrome c
0022-0728
allegro:1991-2014
10082780
Journal of Electroanalytical Chemistry. - ISSN: 0022-0728. - 393 (1995), 1-2, S. 131 - 135
Manfred Paeschke
Rainer Hintsche
Ursula Wollenberger
Wen Jin
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
31773
2009
2009
eng
article
1
--
--
--
Direct electrochemistry and spectroelectrochemistry of osmium substituted horseradish peroxidase
In this contribution the substitution of the central protoporphyrin IX iron complex of horseradish peroxidase by the respective osmium porphyrin complex is described. The direct electrochemical reduction of the Os containing horseradish peroxidase (OsHRP) was achieved at ITO and modified glassy carbon electrodes and in combination with spectroscopy revealed the three redox couples (OsHRP)-H-III/(OsHRP)-H-IV, (OsHRP)-H-IV/(OsHRP)-H-V and (OsHRP)-H-V/ (OsHRP)-H-VI. The midpoint potentials differ dependent on the electrode material used with E-1/2 (Os-III/IV) of -0.4 V (ITO) and -0.25 V (GC), E-1/2 (Os-IV/V) of -0.16 V (ITO) and +0.10 V (GC), and E-1/2 (Os-V/VI)of +018 V (ITO), respectively Moreover, with immobilised OsHRP the direct electrocatalytic reduction of hydrogen peroxide and tert-butyl hydroperoxide was observed. In comparison to electrodes modified with native HRP the sensitivity of the OsHRP-electrode for tert-butyl hydroperoxide is higher.
http://www.sciencedirect.com/science/journal/15675394
10.1016/j.bioelechem.2009.03.015
1567-5394
allegro:1991-2014
10108117
Bioelectrochemistry. - ISSN 1567-5394. - 76 (2009), 1-2, S. 28 - 33
Noya Loew
Ursula Wollenberger
Frieder W. Scheller
Martin Katterle
Institut für Biochemie und Biologie
Referiert
27380
1995
1995
eng
article
1
--
--
--
Biosensors for analytical microsystems
allegro:1991-2014
10082822
Microsystem Technologies. - 1 (1995), S. 75 - 83
Ursula Wollenberger
R. Hintsche
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
27381
1995
1995
eng
article
1
--
--
--
Electrochemical biosensors - ways to improve sensor performance
allegro:1991-2014
10082824
Biotechnology and Genetic Engineering Reviews. - (1995), S. 237 - 266
Ursula Wollenberger
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
22328
1998
1998
eng
article
1
--
--
--
Sensitive catecholamine measurement using a monoenzymatic recycling system
allegro:1991-2014
10093426
Analytica chimica acta. - 368 (1998), 3, S. 233 - 241
Fred Lisdat
Ursula Wollenberger
Manfred Paeschke
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
27738
1995
1995
eng
article
1
--
--
--
Enzyme - based electrodes
allegro:1991-2014
10082803
Encyclopedia of analytical science / Hrsg.: Alan Townshend. - London : Academic Press. - Bd. 2. - 1995. - S. 1190 - 1196
Frieder W. Scheller
Dorothea Pfeiffer
Florian Schubert
Ursula Wollenberger
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
29546
2004
2004
eng
article
1
--
--
--
Direct electron transfer of cytochrome P450 2B4 at electrodes modified with non-ionic detergent and colloidal clay nanoparticles
A method for construction of biosensors with membranous cytochrome P450 isoenzymes was developed based on clay/ detergent/protein mixed films. Thin films of sodium montmorillonite colloid with incorporated cytochrome P450 2134 (CYP2B4) with nonionic detergent were prepared on glassy carbon electrodes. The modified electrodes were electrochemically characterized, and bio-electrocatalytic reactions were followed. CYP2B4 can be reduced fast on clay- modified glassy carbon electrodes in the presence of the nonionic detergent Tween 80. In anaerobic solutions, reversible oxidation and reduction is obtained with a formal potential between -0.292 and - 0.305 V vs Ag/AgCl 1 M KCl depending on the preparation of the biosensor. In air-saturated solution, bio-electrocatalytic reduction currents can be obtained with the CYP2B4-modified electrode on addition of typical substrates such as aminopyrine and benzphetamine. This reaction was suppressed when methyrapone, an inhibitor of P450 reactions, was present. Measurement of product formation also indicates the bioelectrocatialysis by CYP2B4
allegro:1991-2014
10097381
Angewandte Chemie. - 76 (2004), S. 6046 - 6052
V. V. Shumyantseva
Y. D. Ivanov
Nikitas Bistolas
Frieder W. Scheller
Alexander I. Archakov
Ursula Wollenberger
Institut für Biochemie und Biologie
Nicht referiert
32169
2010
2010
eng
article
1
--
--
--
Mesoporous indium tin oxide as a novel platform for bioelectronics
Stable immobilization and reversible electrochemistry of cytochrome c in a tranparent indium tin oxide film with a well-defined mesoporosity (mpITO) is demonstrated. the transparency and good conductivity, in combination with the large surface area of mpITO, allow the incorporation of a high amount of elelctroactive biomolecules and their electrochemical and spectroscopic investigation. UV/Vis and resonance Raman spectroscopy, in combination with direct protein voltammetry are employed for the characterization of cytochrome c immobilized in the mpITO and reveal no perturbant of the structural of the integrity of the redox protein. The potential of this modified material as a biosensor detection of superoxide anions is also demonstrated.
http://www3.interscience.wiley.com/journal/122208635/home
10.1002/cctc.201000047
1867-3880
allegro:1991-2014
10108523
ChemCatChem. - ISSN 1867-3880. - 2 (2010), 7, S. 839 - 845
Stefano Frasca
Till von Graberg
Jiu-Ju Feng
Arne Thomas
Bernd M. Smarsly
Inez M. Weidinger
Frieder W. Scheller
Peter Hildebrandt
Ursula Wollenberger
Institut für Biochemie und Biologie
Referiert
31940
2009
2009
eng
article
1
--
--
--
Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer
An efficient electrocatalytic biosensor for sulfite detection was developed by co-immobilizing sulfite oxidase and cytochrome c with polyaniline sulfonic acid in a layer-by-layer assembly. QCM, UV-Vis spectroscopy and cyclic voltammetry revealed increasing loading of electrochemically active protein with the formation of multilayers. The sensor operates reagentless at low working potential. A catalytic oxidation current was detected in the presence of sulfite at the modified gold electrode, polarized at +0.1 V ( vs. Ag/AgCl 1 M KCl). The stability of the biosensor performance was characterized and optimized. A 17-bilayer electrode has a linear range between 1 and 60 mu M sulfite with a sensitivity of 2.19 mA M-1 sulfite and a response time of 2 min. The electrode retained a stable response for 3 days with a serial reproducibility of 3.8% and lost 20% of sensitivity after 5 days of operation. It is possible to store the sensor in a dry state for more than 2 months. The multilayer electrode was used for determination of sulfite in unspiked and spiked samples of red and white wine. The recovery and the specificity of the signals were evaluated for each sample.
http://www.springerlink.com/content/100417
10.1007/s00216-008-2432-y
1618-2642
allegro:1991-2014
10108291
Analytical and bioanalytical chemistry. - ISSN 1618-2642. - 393 (2009), 1, S. 225 - 233
Roberto Spricigo
Roman Dronov
Fred Lisdat
Silke Leimkühler
Frieder W. Scheller
Ursula Wollenberger
Institut für Biochemie und Biologie
Referiert
23280
1998
1998
eng
article
1
--
--
--
Membrane covered carbon paste electrode for the electrochemical determination of perioxidase and microperoxidase in a flow system
allegro:1991-2014
10088231
Bioelectrochemistry and Bioenergetics. - 45 (1998), 2, S. 227 - 232
J. Kulys
A. Drungiliene
Ursula Wollenberger
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
23282
1998
1998
eng
article
1
--
--
--
Development of a biomimetic alkane sensor f
allegro:1991-2014
10088235
Electrochimica acta. - 43 (1998), S. 3581 - 3585
Ursula Wollenberger
B. Neumann
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
28725
1994
1994
eng
article
1
--
--
--
Enzyme and microbial sensors for phosphate, phenols, pesticides and peroxides
allegro:1991-2014
10082825
Fresenius' Journal of Analytical Chemistry. - 348 (1994), S. 563 - 566
Ursula Wollenberger
B. Neumann
K. Riedel
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
25987
1996
1996
eng
article
1
--
--
--
Overview of biosensor technology : proceedings of Mosbach Symposion on Biochemical Technology
allegro:1991-2014
10082806
Advances in Molecular and Cell Biology. - 15 (1996), S. 351 - 361
Frieder W. Scheller
Ursula Wollenberger
Dorothea Pfeiffer
Florian Schubert
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
31205
2007
2007
eng
article
1
--
--
--
Development of a biosensor for glycated hemoglobin
The development of an electrochemical piezoelectric sensor for the detection of glycated hemoglobin is presented. The total hemoglobin (Hb) content is monitored with a mass-sensitive quartz crystal modified with surfactants, and the glycated fraction of the immobilized Hb is determined by subsequent voltarnmetric measurement of the coupled ferroceneboronic acid. Different modifications of the sensor were tested for their hemoglobin binding ability. Deoxycholate (DOCA) was found to be the most suitable among the examined modifiers. Piezoelectric quartz crystals with gold electrodes were modified with DOCA by covalent binding to a pre-formatted 4-aminothiophenol monolayer. The properties of the Hb binding to DOCA and the pH effect on this interaction were studied. In the proposed assay for glycated hemoglobin at first an Hb sample is incubated with ferroceneboronic acid (FcBA), which binds to the fructosyl residue of the glycated Hb. Then this preincubated Hb sample is allowed to interact with the DOCA-modified piezoelectric quartz crystal. The binding is monitored by quartz crystal nanobalance QCN). The amount of FcBA present on the sensor surface is determined by square wave voltammetry. The binding of FcBA results in well-defined peaks with an EO' of +200 mV versus Ag/AgC1 (1 M KC1). The peak height depends on the degree of glycated Hb in the sample ranging from 0% to 20% of total Hb. The regeneration of the sensing surface is achieved by pepsin digestion of the deposited Hb. Thus the sensor can be re-used more than 30 times.
http://www.sciencedirect.com/science/journal/00134686
10.1016/j.electacta.2007.03.059
0013-4686
allegro:1991-2014
10103440
Electrochimica acta. - ISSN 0013-4686. - 53 (2007), 3, S. 1127 - 1133
Jan Halámek
Ursula Wollenberger
Walter F. M. Stöcklein
Frieder W. Scheller
Institut für Biochemie und Biologie
Referiert
31206
2007
2007
eng
article
1
--
--
--
Signal amplification in immunoassays using labeling via boronic acid binding to the sugar moiety of immunoglobulin G : proof of concept for glycated hemoglobin
A novel electrochemical immunoassay based on the multiple affinity labeling of the indicator antibody with an electro-active tag is presented. The concept is illustrated for the determination of the glycated hemoglobin HbA1c in hemoglobin samples. Hemoglobin is adsorbed to the surfactant-modified surface of a piezoelectric quartz crystal. Whereas the quartz crystal nanobalance is used to validate the total Hb binding, the HbA1c on the sensor surface is recognized by an antibody and quantified electrochemically after the sugar moieties of the antibody have been labeled in-situ with ferroceneboronic acid. The sensitivity of this sensor is about threefold higher than the sensitivity of a hemoglobin sensor, where the ferroceneboronic acid is bound directly to HbA1c.
http://www.informaworld.com/openurl?genre=journal&issn=0003-2719
10.1080/00032710701327096
0003-2719
allegro:1991-2014
10103441
Analytical letters. - ISSN 0003-2719. - 40 (2007), 7, S. 1434 - 1444
Jan Halámek
Ursula Wollenberger
Walter F. M. Stöcklein
Axel Warsinke
Frieder W. Scheller
Institut für Biochemie und Biologie
Referiert
34609
2013
2013
eng
63
72
10
110
article
PERGAMON-ELSEVIER SCIENCE LTD
OXFORD
1
--
--
--
Sensors based on cytochrome P450 and CYP mimicking systems
Cytochrome P450 enzymes (CYPs) act on more than 90 percent of all drugs currently on the market. The catalytic cycle requires electron supply to the heme iron in the presence of oxygen. Electrochemistry allows to characterise the reaction mechanism of these redox enzymes by observing the electron transfer in real time. According to the number of publications on protein electrochemistry CYP has the third position after glucose oxidase and cytochrome c. CYP based enzyme electrodes for the quantification of drugs, metabolites or pesticides have been developed using different iso-enzymes. A crucial step in the sensor development is the efficiency of coupling the biocatalytic systems with the electrode is. In the 1970s the direct electron transfer of heme and heme peptides called microperoxidases (MPs) was used as model of oxidoreductases. They exhibit a broad substrate spectrum including hydroxylation of selected aromatic substrates, demethylation and epoxidation by means of hydrogen peroxide. It overlaps with that of P450 making heme and MPs to alternate recognition elements in biosensors for the detection of typical CYP substrates. In these enzyme electrodes the signal is generated by the conversion of all substrates thus representing in complex media an overall parameter. By combining the biocatalytic substrate conversion with selective binding to a molecularly imprinted polymer layer the specificity has been improved. Here we discuss different approaches of biosensors based on CYP, microperoxidases and catalytically active MIPs and discuss their potential as recognition elements in biosensors. The performance of these sensors and their further development are discussed. (C) 2013 Elsevier Ltd. All rights reserved.
ELECTROCHIMICA ACTA
10.1016/j.electacta.2013.03.154
0013-4686
1873-3859
wos:2011-2013
WOS:000329530300010
Scheller, FW (reprint author), Fraunhofer Inst Biomed Engn IBMT, Muhlenberg 13, D-14476 Potsdam, Germany.
, fschell@uni-potsdam.de
Deutsche Forschungsgemeinschaft (DFG) within the framework of the German
Excellence Initiative [EXC 314]
Aysu Yarman
Ursula Wollenberger
Frieder W. Scheller
eng
uncontrolled
Cytochrome P450
eng
uncontrolled
Microperoxidases
eng
uncontrolled
Catalytically active molecularly imprinted polymers
eng
uncontrolled
Biosensors
eng
uncontrolled
Personalised medicine
34610
2013
2013
eng
172
180
9
2
110
article
PERGAMON-ELSEVIER SCIENCE LTD
OXFORD
1
--
--
--
Bioelectrocatalysis at mesoporous antimony doped tin oxide
electrodes-Electrochemical characterization and direct enzyme
communication
In this paper we report immobilization and bioelectrocatalysis of human sulfite oxidase (hSO) on nanostructured antimony doped tin oxide (ATO) thin film electrodes. Two types of ATO thin film electrodes were prepared via evaporation induced self-assembly of ATO nanoparticle sols. The use of a porogen results in different porosity and film thickness. Nevertheless both electrode types reveal similar quasi reversible electrochemical behavior for positive and negatively charged small mediators. Facile and durable immobilization of catalytically active enzyme in a direct electron transfer configuration was achieved without further chemical modification of the ATO surfaces. Interestingly, the binding of hSO onto the ATO surface seems to be not only of electrostatic nature, but also originates from a strong interaction between the histidine-tag of the enzyme and the supporting material. This is suggested from stable sulfite dependent bioelectrocatalytic signals at high ionic strength and imidazole desorption experiments. As such, ATO appears as a promising conductive platform for the immobilization of complex enzymes and their application in bioelectrocatalysis. (C) 2013 Elsevier Ltd. All rights reserved.
ELECTROCHIMICA ACTA
10.1016/j.electacta.2013.03.144
0013-4686
1873-3859
wos:2011-2013
WOS:000329530300024
Fischer, A (reprint author), Tech Univ Berlin, Inst Chem, Str 17,Juni 135,Haus TK01, D-10623 Berlin, Germany.
, stefano.frasca@uni-potsdam.de; ana.i.moleromilan@campus.tu-berlin.de;
amandine@mail.tu-berlin.de; caren.goebel@tu-berlin.de;
perezf@ebv.org.ve; kstiba@uni-potsdam.de; sleim@uni-potsdam.de;
anna.fischer@tu-berlin.de; uwollen@uni-potsdam.de
Deutsche Forschungsgemeinschaft [EXC 314]; DFG [SM 199/7-1]; European
Union (EFRE) [ILB-Brandenburg 80136126]; BMBF [03IS2201B]; Cluster of
Excellence "Unifying Concepts in Catalysis"
Stefano Frasca
Anabel Molero Milan
Amandine Guiet
Caren Goebel
Fernando Perez-Caballero
Konstanze Stiba
Silke Leimkühler
Anna Fischer
Ursula Wollenberger
eng
uncontrolled
Antimony doped tin dioxide
eng
uncontrolled
Sulfite oxidase
eng
uncontrolled
Direct electrochemistry
eng
uncontrolled
Biosensor
eng
uncontrolled
Bioelectrocatalysis
34572
2013
2013
eng
7
12
6
47
94
article
Elsevier
Lausanne
1
--
--
--
Electrochemically driven biocatalysis of the oxygenase domain of neuronal nitric oxide synthase in indium tin oxide nanoparticles/polyvinyl alcohol nanocomposite
Nitric oxide synthase (NOS) plays a critical role in a number of key physiological and pathological processes. Investigation of electron-transfer reactions in NOS would contribute to a better understanding of the nitric oxide (NO) synthesis mechanism. Herein, we describe an electrochemically driven catalytic strategy, using a nanocomposite that consisted of the oxygenase domain of neuronal NOS (D290nNOSoxy), indium tin oxide (ITO) nanopartides and polyvinyl alcohol (PVA). Fast direct electron transfer between electrodes and D290nNOSoxy was observed with the heterogeneous electron transfer rate constant (k(er)) of 154.8 +/- 0.1 s(-1) at the scan rate of 5 V s(-1). Moreover, the substrate IV-hydroxy-L-arginine (NHA) was used to prove the concept of electrochemically driven biocatalysis of D290nNOSoxy. In the presence of the oxygen cosubstrate and tetrahydrobiopterin (BH4) cofactor, the addition of NHA caused the decreases of both oxidation current at + 0.1 V and reduction current at potentials ranging from -0.149 V to -0.549 V vs Ag/AgCl. Thereafter, a series of control experiments such as in the absence of BH4 or D290nNOSoxy were performed. All the results demonstrated that D290nNOSoxy biocatalysis was successfully driven by electrodes in the presence of BH4 and oxygen. This novel bioelectronic system showed potential for further investigation of NOS and biosensor applications. (C) 2013 Elsevier B.V. All rights reserved.
Bioelectrochemistry : an international journal devoted to electrochemical aspects of biology and biological aspects of electrochemistry ; official journal of the Bioelectrochemical Society
10.1016/j.bioelechem.2013.04.005
1567-5394
1521-186X
wos:2011-2013
WOS:000326561300002
Liu, SQ (reprint author), Southeast Univ, Sch Chem & Chem Engn, Nanjing 211189, Jiangsu, Peoples R China., uwollen@uni-potsdam.de; liusq@seu.edu.cn
National Natural Science Foundation of China [21035002, 21175021];
National Basic Research Program of China [2010CB732400]; Foundation for
Excellent Doctoral Dissertation from Southeast University [YBJJ1112];
Scholarship Award for Excellent Doctoral Student; Ministry of Education;
DAAD; Unicat Cluster of Excellence; Deutsche Forsthungsgemeinschaft
Xuan Xu
Ursula Wollenberger
Jing Qian
Katrin Lettau
Christiane Jung
Songqin Liu
eng
uncontrolled
Nitric oxide synthase
eng
uncontrolled
Tetrahydrobiopterin
eng
uncontrolled
N-omega-hydroxy-L-arginine
eng
uncontrolled
Indium tin oxide nanoparticles
eng
uncontrolled
Biocatalysis
Institut für Biochemie und Biologie
Referiert
34542
2013
2013
eng
5
7
3
37
article
Elsevier
New York
1
--
--
--
Analysis of the interaction of the molybdenum hydroxylase PaoABC from Escherichia coli with positively and negatively charged metal complexes
An unusual behavior of the periplasmic aldehyde oxidoreductase (PaoABC) from Escherichia coil has been observed from electrochemical investigations of the enzyme catalyzed oxidation of aromatic aldehydes with different mediators under different conditions of ionic strength. The enzyme has similarity to other molybdoenzymes of the xanthine oxidase family, but the catalytic behavior turned out to be very different. Under steady state conditions the turnover of PaoABC is maximal at pH 4 for the negatively charged ferricyanide and at pH 9 for a positively charged osmium complex. Stopped-flow kinetic measurements of the catalytic half reaction showed that oxidation of benzaldehyde proceeds also above pH 7. Thus, benzaldehyde oxidation can proceed under acidic and basic conditions using this enzyme, a property which has not been described before for molybdenum hydroxylases. It is also suggested that the electron transfer with artificial electron acceptors and PaoABC can proceed at different protein sites and depends on the nature of the electron acceptor in addition to the ionic strength. (C) 2013 Elsevier B.V. All rights reserved.
Electrochemistry communications : an international journal dedicated to rapid publications in electrochemistry
10.1016/j.elecom.2013.09.017
1388-2481
1873-1902
wos:2011-2013
WOS:000329085700002
Wollenberger, U (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknechtstr 24-25, D-14476 Golm, Germany., uwollen@uni-potsdam.de
Custer of Excellence "UniCat"; DFG [EXC 314]; Taschentuchlabor IZIB;
BMBF [03IS2201B, 03IS2201F]
Artavazd Badalyan
Etienne Galemou Yoga
Viola Schwuchow
Sascha Pöller
Wolfgang Schuhmann
Silke Leimkühler
Ursula Wollenberger
eng
uncontrolled
Electron transfer
eng
uncontrolled
Multi-cofactor enzymes
eng
uncontrolled
Molybdoenzymes
eng
uncontrolled
Aldehyde oxidoreductase
Institut für Biochemie und Biologie
Referiert
23218
1998
1998
eng
article
1
--
--
--
Bioelectrocatalysis by a selenoenzyme
allegro:1991-2014
10088207
Journal of Electroanalytical Chemistry. - 455 (1998), S. 259 - 263
Claudia Lehmann
Ursula Wollenberger
Regina Brigelius-Flohé
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
23271
1998
1998
eng
article
1
--
--
--
PQQ as redox shuttle for quinoprotein glucose dehydrogenase
allegro:1991-2014
10088233
Biological chemistry. - 379 (1998), 8-9, S. 1207 - 1211
Wen Jin
Ursula Wollenberger
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
23274
1998
1998
eng
article
1
--
--
--
Application of a sensitive catechol detector for determination of tyrosinase inhibitors
allegro:1991-2014
10088215
Analytica chimica acta. - 362 (1998), S. 81 - 90
Katrin Streffer
Helvi Kaatz
Christian G. Bauer
Alexander Makower
Thomas Schulmeister
Frieder W. Scheller
Martin G. Peter
Ursula Wollenberger
Institut für Chemie
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
Institut für Organische Chemie und Strukturanalytik
23266
1998
1998
deu
article
1
--
--
--
Funktionalisierung von Elektroden für den direkten heterogenen Elektrotransfer
allegro:1991-2014
10088258
Chemie- und Biosensoren : aktuelle Anwendungen und Entwicklungstrends / 3. Dresdner Sensor-Symposium, 8. - 10. Dezember 1997, Dresden-Radebeul ; Hrsg.: J. P. Baselt ... - Dresden : Univ. Press, 1998. - (Dresdner Beiträge zur Sensorik ; 5). - S. 11 ff
Ursula Wollenberger
Wen Jin
Rita Bernhardt
Claudia Lehmann
Walter F. M. Stöcklein
Regina Brigelius-Flohé
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
23268
1998
1998
eng
article
1
--
--
--
Recycling systems based on screen-printed electrodes
allegro:1991-2014
10088197
Electroanalysis. - 10 (1998), 12, S. 803 - 807
Fred Lisdat
Wah O. Ho
Ursula Wollenberger
Frieder W. Scheller
Torsten Richter
Ursula Bilitewski
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
26267
1996
1996
eng
article
1
--
--
--
Reactive groups on polymer covered electrodes, 4. Lactate-oxidase-biosensor based on electrodes modifies by polyphiophene
allegro:1991-2014
10088192
Macromolecular chemistry and physics. - 197 (1996), S. 3355 - 3363
H.-P. Welzel
G. Kossmehl
G. Engelmann
B. Neumann
Ursula Wollenberger
Frieder W. Scheller
W. Schröder
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
26268
1996
1996
eng
article
1
--
--
--
Electrochemical sensors : enzyme electrodes and field effect transistors
allegro:1991-2014
10088247
Handbook of chemical and biological sensors / Hrsg.: Richard F. Taylor ... - Bristol : Inst. of Physics Publ., 1996. - S. 435 - 458
Dorothea Pfeiffer
Frank Schubert
Ursula Wollenberger
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
29095
1993
1993
eng
article
1
--
--
--
Multienzyme biosensors : coupled enzyme reactions and enzyme activation
allegro:1991-2014
10088189
Uses of immobilized biological compounds / Hrsg.: Georg G. Guilbault ; M. Mascini. - Dodrecht : Kluver, 1993. - (NATO:[Nato ASI series/E] ; 252). - S. 171 - 179
Frieder W. Scheller
Ursula Wollenberger
Florian Schubert
Dorothea Pfeiffer
Alexander Markower
C. J. McNeil
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
29099
1993
1993
eng
article
1
--
--
--
Enhancing biosensor performance using multienzyme systems
allegro:1991-2014
10088185
Trends in biotechnology : TIBTECH. - 11 (1993), Juni, S. 255 - 262
Ursula Wollenberger
Florian Schubert
Dorothea Pfeiffer
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
29100
1993
1993
eng
article
1
--
--
--
Enzyme activation for activator and enzyme activity measurement
allegro:1991-2014
10088186
Biosensors & bioelectronics. - 8 (1993), S. 291 - 297
Ursula Wollenberger
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
29103
1993
1993
eng
article
1
--
--
--
Enzyme and microbial sensors for environmental Monitoring
allegro:1991-2014
10088190
Internatonale conference on Monitoring of toxic chemicals and biomarkers : 23 - 26 June 1992, Berlin, FRG. - Bellingham, Wash. : SPIE, 1993. - (SPIE proceedings series ; 1716 ; EUROPTOP series). - S. 166 - 175
Ursula Wollenberger
B. Neumann
Frieder W. Scheller
Institut für Biochemie und Biologie
Institut für Biochemie und Molekulare Physiologie
37579
2014
2014
eng
2043
2048
6
9
26
article
Wiley-VCH
Weinheim
1
--
--
--
Third generation ATP sensor with enzymatic analyte recycling
For the first time the direct electron transfer of an enzyme - cellobiose dehydrogenase, CDH - has been coupled with the hexokinase catalyzed competition for glucose in a sensor for ATP. To enhance the signal output for ATP, pyruvate kinase was coimmobilized to recycle ADP by the phosphoenolpyruvate driven reaction. The new sensor overcomes the limit of 1:1 stoichiometry of the sequential or competitive conversion of ATP by effective enzymatic recycling of the analyte. The anodic oxidation of the glucose converting CDH proceeds at electrode potentials below 0 mV vs. Ag vertical bar AgCl thus potentially interfering substances like ascorbic acid or catecholamines do not influence the measuring signal. The combination of direct electron transfer of CDH with the enzymatic recycling results in an interference-free and oxygen-independent measurement of ATP in the lower mu molar concentration range with a lower limit of detection of 63.3 nM (S/N=3).
Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
10.1002/elan.201400231
1040-0397
1521-4109
wos:2014
WOS:000343926700023
Yarman, A (reprint author), Fraunhofer Inst Cell Therapy & Immunol IZI, Branch Bioanalyt & Bioprocesses IZI BB, Muhlenberg 13, D-14476 Potsdam, Germany., aysu.yarman@yahoo.de; fschell@uni-potsdam.de
Deutsche Forschungsgemeinschaft (DFG) within the framework of the German
Excellence Initiative [EXC 314]; BMBF in TERA-Sens [93719903]; Swedish
Research Council [2010-5031]; European Commission
[FP7-PEOPLE-2010-ITN-264772]
Aysu Yarman
Christopher Schulz
Cristoph Sygmund
Roland Ludwig
Lo Gorton
Ursula Wollenberger
Frieder W. Scheller
eng
uncontrolled
ATP
eng
uncontrolled
Third generation sensor
eng
uncontrolled
Enzymatic recycling
eng
uncontrolled
Cellobiose dehydrogenase
eng
uncontrolled
Hexokinase
eng
uncontrolled
Pyruvate kinase
Institut für Biochemie und Biologie
Referiert
39003
2015
2015
eng
39
42
4
66
article
Elsevier
Oxford
1
--
--
--
Miniature direct electron transfer based sulphite/oxygen enzymatic fuel cells
A direct electron transfer (DET) based sulphite/oxygen biofuel cell is reported that utilises human sulphite oxidase (hSOx) and Myrothecium verrucaria bilirubin oxidase (MvBOx) and nanostructured gold electrodes. For bioanode construction, the nanostructured gold microelectrodes were further modified with 3,3'-dithiodipropionic acid di(N-hydroxysuccinimide ester) to which polyethylene imine was covalently attached. hSOx was adsorbed onto this chemically modified nanostructured electrode with high surface loading of electroactive enzyme and in presence of sulphite high anodic bioelectrocatalytic currents were generated with an onset potential of 0.05 V vs. NHE. The biocathode contained MyBOx directly adsorbed to the deposited gold nanoparticles for cathodic oxygen reduction starting at 0.71 V vs. NHE. Both enzyme electrodes were integrated to a DET-type biofuel cell. Power densities of 8 and 1 mu W cm(-2) were achieved at 0.15 V and 0.45 V of cell voltages, respectively, with the membrane based biodevices under aerobic conditions. (C) 2014 Elsevier B.V. All rights reserved.
Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics
10.1016/j.bios.2014.10.080
25460879
0956-5663
1873-4235
wos:2015
WOS:000348619800006
Shleev, S (reprint author), Malmo Univ, S-20506 Malmo, Sweden., sergey.shleev@mah.se; uwollen@uni-potsdam.de
Russian Scientific Foundation [14-14-00530]; Deutsche
Forschungsgemeinschaft (Unicat Cluster of Excellence) [EXC 314/2];
ILB-Brandenburg [80136126]; BMBF [03IS2201B]
Ting Zeng
Dmitry Pankratov
Magnus Falk
Silke Leimkühler
Sergey Shleev
Ursula Wollenberger
eng
uncontrolled
Enzymatic fuel cell
eng
uncontrolled
Microscale electrode
eng
uncontrolled
Direct electron transfer
eng
uncontrolled
Sulphite oxidase
eng
uncontrolled
Bilirubin oxidase
Institut für Biochemie und Biologie
Referiert
39029
2015
2015
eng
938
944
7
4
27
article
Wiley-VCH
Weinheim
1
--
--
--
A pH Responsive Redox Hydrogel for Electrochemical Detection of Redox Silent Biocatalytic Processes. Control of Hydrogel Solvation
The control of bioelectrocatalytic processes by external stimuli for the indirect detection of non-redox active species was achieved using an esterase and a redox enzyme both integrated within a redox hydrogel. The poly( vinyl) imidazole Os(bpy)(2)Cl hydrogel displays pH-responsive properties. The esterase catalysed reaction leads to a local pH decrease causing protonation of imidazole moieties thus increasing hydrogel solvation and mobility of the tethered Os-complexes. This is the key step to enable improved electron transfer between an aldehyde oxidoreductase and the polymer-bound Os-complexes. The off-on switch is further integrated in a biofuel cell system for self-powered signal generation.
Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
10.1002/elan.201400621
1040-0397
1521-4109
wos:2015
WOS:000354198400013
Plumere, N (reprint author), Ruhr Univ Bochum, Ctr Electrochem Sci CES Mol Nanostruct, D-44780 Bochum, Germany., nicolas.plumere@rub.de; wolfgang.schuhmann@rub.de
Cluster of Excellence RESOLV - Deutsche Forschungsgemeinschaft (DFG)
[EXC 1069]; Unicat - Deutsche Forschungsgemeinschaft (DFG) [EXC 314/2];
Bundesministerium fur Bildung und Forschung (BMBF) within the Project
Taschentuchlabor [03IS2201B, 03IS2201F]
Andrea Contin
Stefano Frasca
Jeevanthi Vivekananthan
Silke Leimkühler
Ursula Wollenberger
Nicolas Plumere
Wolfgang Schuhmann
eng
uncontrolled
pH responsive hydrogel
eng
uncontrolled
External stimuli
eng
uncontrolled
Biofuel cell
eng
uncontrolled
Self-powered biosensor
eng
uncontrolled
Solvation
Institut für Biochemie und Biologie
Referiert
36744
2011
2011
eng
8309
8315
7
13
27
article
American Chemical Society
Washington
1
--
--
--
Cytochrome c/polyelectrolyte multilayers investigated by E-QCM-D - effect of temperature on the assembly structure
Protein multilayers, consisting of cytochrome c (cyt c) and poly(aniline sulfonic acid) (PASA), are investigated by electrochemical quartz crystal microbalance with dissipation monitoring (E-QCM-D). This technique reveals that a four-bilayer assembly has rather rigid properties. A thickness of 16.3 +/- 0.8 nm is calculated with the Sauerbrey equation and is found to be in good agreement with a viscoelastic model. The electroactive amount of cyt c is estimated by the deposited mass under the assumption of 50% coupled water. Temperature-induced stabilization of the multilayer assembly has been investigated in the temperature range between 30 and 45 degrees C. The treatment results in a loss of material and a contraction of the film. The electroactive amount of cyt c also decreases during heating and remains constant after the cooling period. The contraction of the film is accompanied by the enhanced stability of the assembly. In addition, it is found that cyt c and PASA can be assembled at higher temperatures, resulting in the formation of multilayer systems with less dissipation.
Langmuir
10.1021/la200860p
0743-7463
wos:2011-2013
WOS:000292124000044
Lisdat, F (reprint author), Wildau Univ Appl Sci, Bahnhofstr 1, D-15745 Wildau, Germany.
Ministerium fur Wissenschaft, Forschung und Kultur, Brandenburg, Germany
[3508-14/13]; BMBF [IZIB 03IS2201B]; DFG (Unicat Cluster of Excellence,
EXC) [314]
Christian Kepplinger
Fred Lisdat
Ursula Wollenberger
Institut für Biochemie und Biologie
Referiert
38199
2014
2014
eng
63761
63771
11
109
4
article
Royal Society of Chemistry
Cambridge
1
--
--
--
A compact multifunctional microfluidic platform for exploring cellular dynamics in real-time using electrochemical detection
Downscaling of microfluidic cell culture and detection devices for electrochemical monitoring has mostly focused on miniaturization of the microfluidic chips which are often designed for specific applications and therefore lack functional flexibility. We present a compact microfluidic cell culture and electrochemical analysis platform with in-built fluid handling and detection, enabling complete cell based assays comprising on-line electrode cleaning, sterilization, surface functionalization, cell seeding, cultivation and electrochemical real-time monitoring of cellular dynamics. To demonstrate the versatility and multifunctionality of the platform, we explored amperometric monitoring of intracellular redox activity in yeast (Saccharomyces cerevisiae) and detection of exocytotically released dopamine from rat pheochromocytoma cells (PC12). Electrochemical impedance spectroscopy was used in both applications for monitoring cell sedimentation and adhesion as well as proliferation in the case of PC12 cells. The influence of flow rate on the signal amplitude in the detection of redox metabolism as well as the effect of mechanical stimulation on dopamine release were demonstrated using the programmable fluid handling capability. The here presented platform is aimed at applications utilizing cell based assays, ranging from e.g. monitoring of drug effects in pharmacological studies, characterization of neural stem cell differentiation, and screening of genetically modified microorganisms to environmental monitoring.
RSC Advances
10.1039/c4ra12632g
2046-2069
wos:2014
WOS:000345702900020
Emneus, J (reprint author), Tech Univ Denmark, Dept Micro & Nanotechnol, Prod Torvet 423, DK-2800 Lyngby, Denmark., Jenny.Emneus@nanotech.dtu.dk
EU [NMP4-SL-2008-214706]; Danish Council for Independent Research
Natural Sciences; Lundbeck Foundation [R69-A6408]; Department of Micro-
and Nanotechnology, Technical University of Denmark
K. Zor
A. Heiskanen
Claudia Caviglia
M. Vergani
E. Landini
F. Shah
Marco Carminati
A. Martinez-Serrano
T. Ramos Moreno
M. Kokaia
Dafna Benayahu
Zs. Keresztes
D. Papkovsky
Ursula Wollenberger
W. E. Svendsen
M. Dimaki
G. Ferrari
R. Raiteri
M. Sampietro
M. Dufva
Jenny Emneus
Institut für Biochemie und Biologie
Referiert
38209
2014
2014
eng
43092
43097
6
81
4
article
Royal Society of Chemistry
Cambridge
1
--
--
--
Surface modification with thermoresponsive polymer brushes for a switchable electrochemical sensor
Elaboration of switchable surfaces represents an interesting way for the development of a new generation of electrochemical sensors. In this paper, a method for growing thermoresponsive polymer brushes from a gold surface pre-modified with polyethyleneimine (PEI), subsequent layer-by-layer polyelectrolyte assembly and adsorption of a charged macroinitiator is described. We propose an easy method for monitoring the coil-to-globule phase transition of the polymer brush using an electrochemical quartz crystal microbalance with dissipation (E-QCM-D). The surface of these polymer modified electrodes shows reversible switching from the swollen to the collapsed state with temperature. As demonstrated from E-QCM-D measurements using an original signal processing method, the switch is operating in three reversible steps related to different interfacial viscosities. Moreover, it is shown that the one electron oxidation of ferrocene carboxylic acid is dramatically affected by the change from the swollen to the collapsed state of the polymer brush, showing a spectacular 86% decrease of the charge transfer resistance between the two states.
RSC Advances
10.1039/c4ra07190e
2046-2069
wos:2014
WOS:000344525500044
Wollenberger, U (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25,Haus 25, D-14476 Potsdam, Germany., uwollen@uni-potsdam.de
Bundesministerium fur Bildung und Forschung BMBF (German Federal
Ministry of Education and Research), Initiative "Spitzenforschung &
Innovation in den neuen Landern" ("Das Taschentuchlabor") [FKZ
03IS2201B]
Clement Comminges
Stefano Frasca
Martin Suetterlin
Erik Wischerhoff
André Laschewsky
Ursula Wollenberger
Institut für Chemie
Referiert
38818
2015
2015
eng
1960
1968
9
9
16
article
Wiley-VCH
Weinheim
1
--
--
--
Spectroscopic Observation of Calcium-Induced Reorientation of Cellobiose Dehydrogenase Immobilized on Electrodes and its Effect on Electrocatalytic Activity
Cellobiose dehydrogenase catalyzes the oxidation of various carbohydrates and is considered as a possible anode catalyst in biofuel cells. It has been shown that the catalytic performance of this enzyme immobilized on electrodes can be increased by presence of calcium ions. To get insight into the Ca2+-induced changes in the immobilized enzyme we employ surface-enhanced vibrational (SERR and SEIRA) spectroscopy together with electrochemistry. Upon addition of Ca2+ ions electrochemical measurements show a shift of the catalytic turnover signal to more negative potentials while SERR measurements reveal an offset between the potential of heme reduction and catalytic current. Comparing SERR and SEIRA data we propose that binding of Ca2+ to the heme induces protein reorientation in a way that the electron transfer pathway of the catalytic FAD center to the electrode can bypass the heme cofactor, resulting in catalytic activity at more negative potentials.
ChemPhysChem : a European journal of chemical physics and physical chemistry
10.1002/cphc.201500112
25908116
1439-4235
1439-7641
wos:2015
WOS:000356714800023
Weidinger, IM (reprint author), Tech Univ Berlin, Inst Chem, Str 17 Juni 135, D-10623 Berlin, Germany., inez.weidinger@tu-berlin.de
DFG (BIG-NSE, Unicat) [SFB 1078]; Programm zur Berliner
Chancengleichheit (BCP); Swedish Research Council [2010-5031,
2014-5908]; European Commission [FP7-PITN-GA-2010-264772,
FP7-PEOPLE-2013-ITN-607793]
Patrycja Kielb
Murat Sezer
Sagie Katz
Francesca Lopez
Christopher Schulz
Lo Gorton
Roland Ludwig
Ursula Wollenberger
Ingo Zebger
Inez M. Weidinger
eng
uncontrolled
cellobiose dehydrogenase
eng
uncontrolled
electron transfer
eng
uncontrolled
enzyme catalysis
eng
uncontrolled
spectroelectrochemistry
eng
uncontrolled
surface-enhanced vibrational spectroscopy
Institut für Biochemie und Biologie
Referiert
38779
2015
2015
eng
3526
3531
6
21
article
Wiley-VCH
Weinheim
1
--
--
--
The Electrically Wired Molybdenum Domain of Human Sulfite Oxidase is Bioelectrocatalytically Active
We report electron transfer between the catalytic molybdenum cofactor (Moco) domain of human sulfite oxidase (hSO) and electrodes through a poly(vinylpyridine)-bound [osmium(N,N'-methyl-2,2'-biimidazole)(3)](2+/3+) complex as the electron-transfer mediator. The biocatalyst was immobilized in this low-potential redox polymer on a carbon electrode. Upon the addition of sulfite to the immobilized separate Moco domain, the generation of a significant catalytic current demonstrated that the catalytic center is effectively wired and active. The bioelectrocatalytic current of the wired separate catalytic domain reached 25% of the signal of the wired full molybdoheme enzyme hSO, in which the heme b(5) is involved in the electron-transfer pathway. This is the first report on a catalytically active wired molybdenum cofactor domain. The formal potential of this electrochemical mediator is between the potentials of the two cofactors of hSO, and as hSO can occupy several conformations in the polymer matrix, it is imaginable that electron transfer from the catalytic site to the electrode through the osmium center occurs for the hSO molecules in which the Moco domain is sufficiently accessible. The observation of catalytic oxidation currents at low potentials is favorable for applications in bioelectronic devices.
European journal of inorganic chemistry : a journal of ChemPubSoc Europe
10.1002/ejic.201500034
1434-1948
1099-0682
wos:2015
WOS:000359297800017
Wollenberger, U (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25, D-14476 Potsdam, Germany., uwollen@uni-potsdam.de
Deutsche Forschungsgemeinschaft (DFG) within German Excellence
Initiative [EXC 314/2]; European Community [COST 1003]; Swedish Research
Council
Roberto Spricigo
Silke Leimkühler
Lo Gorton
Frieder W. Scheller
Ursula Wollenberger
eng
uncontrolled
Metalloenzymes
eng
uncontrolled
Enzyme catalysis
eng
uncontrolled
Immobilization
eng
uncontrolled
Osmium
Institut für Biochemie und Biologie
Referiert
36433
2011
2011
eng
1419
1426
8
1
160
article
Elsevier
Lausanne
1
--
--
--
Direct electron transfer of Agrocybe aegerita peroxygenase at electrodes modified with chitosan-capped Au nanoparticles and its bioelectrocatalysis to aniline
Three different sizes of chitosan-capped Au nanoparticles were synthesized and were used to incorporate Agrocybe aegerita peroxygenase (AaeAPO) onto the surface of glassy carbon electrode. The direct electron transfer of AaeAPO was achieved in all films. The highest amount of electroactive enzyme and highest electron transfer rate constant k(s) of AaeAPO were obtained in the film with the smallest size of chitosan-capped Au nanoparticles.
In anaerobic solutions, quasi-reversible oxidation and reduction are obtained with a formal potential of -0.280V vs. Ag/AgCl 1 M KCl in 100 mM (pH 7.0) PBS at scan rate of 1 V s(-1). Bioelectrocatalytic reduction currents can be obtained with the AaeAPO-modified electrode on addition of hydrogen peroxide. This reaction was suppressed when sodium azide, an inhibitor of AaeAPO, was present. Furthermore, the peroxide-dependent conversion of aniline was characterized and it was found that a polymer product via p-aminophenol is formed. And the AaeAPO biosensor was applied to determine aniline and p-aminophenol.
Sensors and actuators : B, Chemical
10.1016/j.snb.2011.09.090
0925-4005
wos:2011-2013
WOS:000298768100196
Scheller, FW (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25, D-14476 Golm, Germany., fschell@uni-potsdam.de
Deutsche Forschungsgemeinschaft (DFG) [EXC 314]
Yunhua Wu
Ursula Wollenberger
Martin Hofrichter
Rene Ullrich
Katrin Scheibner
Frieder W. Scheller
eng
uncontrolled
Agrocybe aegerita peroxygenase
eng
uncontrolled
Au nanoparticles
eng
uncontrolled
Direct electron transfer
eng
uncontrolled
Aniline biosensor
eng
uncontrolled
Bioelectrocatalysis
Institut für Biochemie und Biologie
Referiert
36435
2011
2011
eng
320
323
4
1
30
article
Elsevier
Oxford
1
--
--
--
Enzyme electrode for aromatic compounds exploiting the catalytic activities of microperoxidase-11
Microperoxidase-11 (MR-11) which has been immobilised in a matrix of chitosan-embedded gold nanoparticles on the surface of a glassy carbon electrode catalyzes the conversion of aromatic substances. This peroxide-dependent catalysis of microperoxidase has been applied in an enzyme electrode for the first time to indicate aromatic compounds such as aniline. 4-fluoroaniline, catechol and p-aminophenol. The electrode signal is generated by the cathodic reduction of the quinone or quinoneimine which is formed in the presence of both MP-II and peroxide from the substrate. The same sensor principle will be extended to aromatic drugs.
Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics
10.1016/j.bios.2011.09.004
0956-5663
wos:2011-2013
WOS:000297610200051
Scheller, FW (reprint author), Univ Potsdam, Dept Analyt Biochem, Inst Biochem & Biol, Liebknechtstr 24-25, D-14476 Golm, Germany., fschell@uni-potsdam.de
BMBF of Germany [0311993]; Deutsche Forschungsgemeinschaft (DFG) within
the German Excellence Initiative [EXC 314]
Aysu Yarman
Artavazd Badalyan
Nenad Gajovic-Eichelmann
Ursula Wollenberger
Frieder W. Scheller
eng
uncontrolled
Microperoxidase-11
eng
uncontrolled
Nanoparticles
eng
uncontrolled
p-Aminophenol
eng
uncontrolled
Aniline
eng
uncontrolled
Catechol
eng
uncontrolled
4-Fluoroaniline
eng
uncontrolled
Biosensors
Institut für Biochemie und Biologie
Referiert
36461
2011
2011
eng
554
558
5
6
11
article
Wiley-Blackwell
Malden
1
--
--
--
Electrochemical switchable protein-based optical device
The present work contributes to the development of reusable sensing systems with a visual evaluation of the detection process related to an analyte. An electrochemical switchable protein-based optical device was designed with the core part composed of cytochrome c immobilized in a mesoporous indium tin oxide film. A color-developing redox-sensitive dye was used as switchable component of the system. The cytochrome c-catalyzed oxidation of the dye by hydrogen peroxide is spectroscopically investigated. When the dye is co-immobilized with the protein, its redox state is easily controlled by application of an electrical potential at the supporting material. This enables to electrochemically reset the system to the initial state and repetitive signal generation. The implemented reset function of the color forming reaction will make calibration of small test devices possible. The principle can be extended to other color forming redox reactions and to coupled enzyme systems, such as rapid food testing and indication of critical concentrations of metabolites for health care.
Engineering in life sciences : Industry, Environment, Plant, Food
10.1002/elsc.201100079
1618-0240
wos:2011-2013
WOS:000298301600003
Wollenberger, U (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25,Haus 25, D-14476 Golm, Germany., uwollen@uni-potsdam.de
Deutsche Forschungsgemeinschaft [EX314]; Bundesminister fur Bildung und
Forschung [03IS2201B]
Stefano Frasca
Claudia Richter
Till von Graberg
Bernd M. Smarsly
Ursula Wollenberger
eng
uncontrolled
Cytochrome c
eng
uncontrolled
Electrochemical switch
eng
uncontrolled
Indium tin oxide
eng
uncontrolled
mesoporous materials
eng
uncontrolled
Optical device
Institut für Biochemie und Biologie
Referiert
38861
2015
2015
eng
1350
1358
9
6
27
article
Wiley-VCH
Weinheim
1
--
--
--
An Electrochemical Assay for Monitoring Differentiation of the Osteoblastic Cell Line (MBA-15) on the Sensor Chip
An electrochemical assay for the indication of the activity of the cell bound differentiation marker alkaline phosphatase (ALP) is proposed using voltammetry on an in-vitro cell culture. The basis of the assay is cultivation of cells on gold microelectrodes in wells of a microplate, catalytic hydrolysis of p-aminophenyl phosphate by ALP and indication of p-aminophenol oxidation by square wave voltammetry (SWV) with the sensors onto which the cells attached. The morphology of the bone marrow stromal cell line (MBA-15) on the electrode surface was investigated and it exhibited in vitro osteogenic characteristics. Since ALP is expressed on the cell surface in early differentiation stage of osteoblastic cells, its activity was followed after different culture times over a period of 144 h by recording repetitive voltammograms at different time points upon addition of the substrate p-aminophenyl phosphate. The ALP activity was estimated from the signal increase related to formation rate of p-aminophenol and the number of cells. The highest value was measured at 120 h, when the cells reached confluence. The results of the electrochemical activity assay are consistent with the colorimetric acquired value from p-nitrophenol formation rate.
Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
10.1002/elan.201400684
1040-0397
1521-4109
wos:2015
WOS:000356604300004
Wollenberger, U (reprint author), Univ Potsdam, Dept Mol Enzymol, Inst Biochem & Biol, D-14469 Potsdam, Germany., uwollen@uni-potsdam.de
European Union (FP7/EXCELL); ILB Brandenburg (TERASENS)
Cigdem Yildirim-Semerci
Dafna Benayahu
Miriam Adamovski
Ursula Wollenberger
eng
uncontrolled
Alkaline phosphatase
eng
uncontrolled
Osteoblast
eng
uncontrolled
Voltammetry
eng
uncontrolled
Biomarker
eng
uncontrolled
p-Aminophenol
Institut für Biochemie und Biologie
Referiert
38934
2015
2015
eng
7596
7602
7
20
21
article
Wiley-VCH
Weinheim
1
--
--
--
Surface-Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine-Coordinated Heme Protein
Molecular modeling, electrochemical methods, and quartz crystal microbalance were used to characterize immobilized hexameric tyrosine-coordinated heme protein (HTHP) on bare carbon or on gold electrodes modified with positively and negatively charged self-assembled monolayers (SAMs), respectively. HTHP binds to the positively charged surface but no direct electron transfer (DET) is found due to the long distance of the active sites from the electrode surfaces. At carboxyl-terminated surfaces, the neutrally charged bottom of HTHP can bind to the SAM. For this "disc" orientation all six hemes are close to the electrode and their direct electron transfer should be efficient. HTHP on all negatively charged SAMs showed a quasi-reversible redox behavior with rate constant k(s) values between 0.93 and 2.86 s(-1) and apparent formal potentials E-app(0)' between -131.1 and -249.1 mV. On the MUA/MU-modified electrode, the maximum surface concentration corresponds to a complete monolayer of the hexameric HTHP in the disc orientation. HTHP electrostatically immobilized on negatively charged SAMs shows electrocatalysis of peroxide reduction and enzymatic oxidation of NADH.
Chemistry - a European journal
10.1002/chem.201405932
25825040
0947-6539
1521-3765
wos:2015
WOS:000354027300039
Scheller, FW (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25, D-14476 Potsdam, Germany., fschell@uni-potsdam.de
Deutsche Forschungsgemeinschaft (DFG) within German Excellence
Initiative [EXC 314]
Lei Peng
Tillmann Utesch
Aysu Yarman
Jae-Hun Jeoung
Silke Steinborn
Holger Dobbek
Maria Andrea Mroginski
Johannes Tanne
Ursula Wollenberger
Frieder W. Scheller
eng
uncontrolled
electrochemistry
eng
uncontrolled
electron transfer
eng
uncontrolled
heme proteins
eng
uncontrolled
molecular modeling
eng
uncontrolled
monolayers
Institut für Biochemie und Biologie
Referiert
36910
2011
2011
eng
1798
1804
7
7
23
article
American Chemical Society
Washington
1
--
--
--
A molecular precursor approach to tunable porous tin-rich indium tin oxide with durable high electrical conductivity for bioelectronic devices
The preparation of porous, i.e., high surface area electrodes from transparent conducting oxides, is a valuable goal in materials chemistry as such electrodes can enable further development of optoelectronic, electrocatalytic, or bioelectronic devices. In this work the first tin-rich mesoporous indium tin oxide is prepared using the molecular heterobimetallic single-source precursor, indium tin tris-tert-butoxide, together with an appropriate structure-directing template, yielding materials with high surface areas and tailorable pore size. The resulting mesoporous tin-rich ITO films show a high and durable electrical conductivity and transparency, making them interesting materials for hosting electroactive biomolecules such as proteins. In fact, its unique performance in bioelectronic applications has been demonstrated by immobilization of high amounts of cytochrome c into the mesoporous film which undergo redox processes directly with the conductive electrode material.
Chemistry of materials : a publication of the American Chemical Society
10.1021/cm103087p
0897-4756
wos:2011-2013
WOS:000289029400022
Driess, M (reprint author), Tech Univ Berlin, Inst Chem Metalorgan & Inorgan Mat, Str 17,Juni 135, D-10623 Berlin, Germany., matthias.driess@tu-berlin.de; arne.thomas@tu-berlin.de
Deutsche Forschungsgemeinschaft; TU Berlin
Yilmaz Aksu
Stefano Frasca
Ursula Wollenberger
Matthias Driess
Arne Thomas
eng
uncontrolled
indium tin oxide ITO
eng
uncontrolled
electrode
eng
uncontrolled
bioelectrochemistry
eng
uncontrolled
device
eng
uncontrolled
cytochrome c
Institut für Biochemie und Biologie
Referiert
37765
2014
2014
eng
8937
8941
5
12
6
article
American Chemical Society
Washington
1
--
--
--
Dendritic polyglycerol-poly(ethylene glycol)-based polymer networks for biosensing application
This work describes the formation of a new dendritic polyglycerol-poly(ethylene glycol)-based 3D polymer network as a matrix for immobilization of the redox enzyme periplasmatic aldehyde oxidoreductase to create an electrochemical biosensor. The novel network is built directly on the gold surface, where it simultaneously stabilizes the enzyme for up to 4 days. The prepared biosensors can be used for amperometric detection of benzaldehyde in the range of 0.8-400 mu M.
ACS applied materials & interfaces
10.1021/am502018x
24882361
1944-8244
wos:2014
WOS:000338184500002
Wollenberger, U (reprint author), Univ Potsdam, Inst Biol & Biochem, Karl Liebknechtstr 24-25, D-14476 Potsdam, Germany., uwollen@uni-potsdam.de; haag@chemie.fu-berlin.de
Cluster of Excellence "UniCAT" (Unifying Concepts in Catalysis, Berlin);
graduate school "BIG NSE"; LB Brandenburg (Terasens)
Pradip Dey
Miriam Adamovski
Simon Friebe
Artavazd Badalyan
Radu-Cristian Mutihac
Florian Paulus
Silke Leimkühler
Ursula Wollenberger
Rainer Haag
eng
uncontrolled
biosensors
eng
uncontrolled
hydrogel
eng
uncontrolled
amperometry
eng
uncontrolled
dendritic
Institut für Biochemie und Biologie
Referiert
38585
2015
2015
eng
21487
21494
8
38
7
article
American Chemical Society
Washington
1
--
--
--
Effective Electrochemistry of Human Sulfite Oxidase Immobilized on Quantum-Dots-Modified Indium Tin Oxide Electrode
The bioelectrocatalytic sulfite oxidation by human sulfite oxidase (hSO) on indium tin oxide (ITO) is reported, which is facilitated by functionalizing of the electrode surface with polyethylenimine (PEI)-entrapped CdS nanoparticles and enzyme. hSO was assembled onto the electrode with a high surface loading of electroactive enzyme. In the presence of sulfite but without additional mediators, a high bioelectrocatalytic current was generated. Reference experiments with only PEI showed direct electron transfer and catalytic activity of hSO, but these were less pronounced. The application of the polyelectrolyte-entrapped quantum dots (QDs) on ITO electrodes provides a compatible surface for enzyme binding with promotion of electron transfer. Variations of the buffer solution conditions, e.g., ionic strength, pH, viscosity, and the effect of oxygen, were studied in order to understand intramolecular and heterogeneous electron transfer from hSO to the electrode. The results are consistent with a model derived for the enzyme by using flash photolysis in solution and spectroelectrochemistry and molecular dynamic simulations of hSO on monolayer-modified gold electrodes. Moreover, for the first time a photoelectrochemical electrode involving immobilized hSO is demonstrated where photoexcitation of the CdS/hSO-modified electrode lead to an enhanced generation of bioelectrocatalytic currents upon sulfite addition. Oxidation starts already at the redox potential of the electron transfer domain of hSO and is greatly increased by application of a small overpotential to the CdS/hSO-modified ITO.
ACS applied materials & interfaces
10.1021/acsami.5b06665
26357959
1944-8244
wos:2015
WOS:000362243500056
Wollenberger, U (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25, D-14476 Potsdam, Germany., uwollen@uni-potsdam.de
Cluster of Excellence "Unifying Concepts in Catalysis" - Deutsche
Forschungsgemeinschaft [EXC 314/2]; ILB-Brandenburg [80136126]; BMBF
[03IS2201B]
Ting Zeng
Silke Leimkühler
Joachim Koetz
Ursula Wollenberger
eng
uncontrolled
human sulfite oxidase
eng
uncontrolled
direct electrochemistry
eng
uncontrolled
bioelectrocatalysis
eng
uncontrolled
photocurrent
eng
uncontrolled
CdS quantum dots
Institut für Biochemie und Biologie
Referiert
35588
2012
2012
eng
498
507
10
5
6
article
Inst. of Electr. and Electronics Engineers
Piscataway
1
--
--
--
Multichannel bipotentiostat integrated with a microfluidic platform for electrochemical real-time monitoring of cell cultures
An electrochemical detection system specifically designed for multi-parameter real-time monitoring of stem cell culturing/differentiation in a microfluidic system is presented. It is composed of a very compact 24-channel electronic board, compatible with arrays of microelectrodes and coupled to a microfluidic cell culture system. A versatile data acquisition software enables performing amperometry, cyclic voltammetry and impedance spectroscopy in each of the 12 independent chambers over a 100 kHz bandwidth with current resolution down to 5 pA for 100 ms measuring time. The design of the platform, its realization and experimental characterization are reported, with emphasis on the analysis of impact of input capacitance (i.e., microelectrode size) and microfluidic pump operation on current noise. Programmable sequences of successive injections of analytes (ferricyanide and dopamine) and rinsing buffer solution as well as the impedimetric continuous tracking for seven days of the proliferation of a colony of PC12 cells are successfully demonstrated.
IEEE Transactions on biomedical circuits and systems
10.1109/TBCAS.2012.2187783
1932-4545
wos:2011-2013
WOS:000313906500011
Vergani, M (reprint author), Politecn Milan, Dipartimento Elettron & Informaz, I-20133 Milan, Italy., vergani@elet.polimi.it; sampietr@elet.polimi.it
EU FP7 EXCELL project [NMP4-SL-2008-214706]
Marco Vergani
Marco Carminati
Giorgio Ferrari
Ettore Landini
Claudia Caviglia
Arto Heiskanen
Clement Comminges
Kinga Zor
David Sabourin
Martin Dufva
Maria Dimaki
Roberto Raiteri
Ursula Wollenberger
Jenny Emneus
Marco Sampietro
eng
uncontrolled
Electrochemical measurements
eng
uncontrolled
impedance spectroscopy
eng
uncontrolled
microfluidics
eng
uncontrolled
multichannel potentiostat
eng
uncontrolled
stem cell monitoring
Institut für Biochemie und Biologie
Referiert
37002
2011
2011
eng
611
618
8
3
23
article
Wiley-Blackwell
Malden
1
--
--
--
Bioelectrocatalysis by Microperoxidase-11 in a Multilayer Architecture of Chitosan Embedded Gold Nanoparticles
We report on the redox behaviour of the microperoxidase-11 (MP-11) which has been electrostatically immobilized in a matrix of chitosan-embedded gold nanoparticles on the surface of a glassy carbon electrode. MP-11 contains a covalently bound heme c as the redox active group that exchanges electrons with the electrode via the gold nanoparticles. Electroactive surface concentration of MP-11 at high scan rate is between 350+/-50 pmol cm(-2), which reflects a multilayer process. The formal potential (E degrees') of MP-11 in the gold nanoparticles-chitosan film was estimated to be -(267.7+/-2.9) mV at pH 7.0. The heterogeneous electron transfer rate constant (k(s)) starts at 1.21 s(-1) and levels off at 6.45 s(-1) in the scan rate range from 0.1 to 2.0 V s(-1). Oxidation and reduction of MP-11 by hydrogen peroxide and superoxide, respectively have been coupled to the direct electron transfer of MP-11.
Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
10.1002/elan.201000535
1040-0397
wos:2011-2013
WOS:000288093400008
Scheller, FW (reprint author), Fraunhofer Inst Biomed Engn, D-14476 Potsdam, Germany., fschell@uni-potsdam.de
BMBF of Germany [0311993]; Deutsche Forschunsgeminschaft (DFG) within
the framework of the German Excellence Initiative [EXC 314]
Aysu Yarman
Thomas Nagel
Nenad Gajovic-Eichelmann
Anna Fischer
Ursula Wollenberger
Frieder W. Scheller
eng
uncontrolled
Microperoxidase
eng
uncontrolled
Direct electron transfer
eng
uncontrolled
Nanoparticles
eng
uncontrolled
Hydrogen peroxide
eng
uncontrolled
Superoxide
eng
uncontrolled
Bioelectrocatalysis
Institut für Chemie
Referiert
35402
2013
2013
eng
101
108
8
1
25
article
Wiley-VCH
Weinheim
1
--
--
--
A Biosensor for aromatic aldehydes comprising the mediator dependent PaoABC-Aldehyde oxidoreductase
A novel aldehyde oxidoreductase (PaoABC) from Escherichia coli was utilized for the development of an oxygen insensitive biosensor for benzaldehyde. The enzyme was immobilized in polyvinyl alcohol and currents were measured for aldehyde oxidation with different one and two electron mediators with the highest sensitivity for benzaldehyde in the presence of hexacyanoferrate(III). The benzaldehyde biosensor was optimized with respect to mediator concentration, enzyme loading and pH using potassium hexacyanoferrate(III). The linear measuring range is between 0.5200 mu M benzaldehyde. In correspondence with the substrate selectivity of the enzyme in solution the biosensor revealed a preference for aromatic aldehydes and less effective conversion of aliphatic aldehydes. The biosensor is oxygen independent, which is a particularly attractive feature for application. The biosensor can be applied to detect contaminations with benzaldehyde in solvents such as benzyl alcohol, where traces of benzaldehyde in benzyl alcohol down to 0.0042?% can be detected.
Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
10.1002/elan.201200362
1040-0397
wos:2011-2013
WOS:000313807600013
Wollenberger, U (reprint author), Univ Potsdam, Inst Biochem & Biol, Dept Mol Enzymol, Karl Liebknechtstr 24-25, D-14476 Potsdam, Germany., uwollen@uni-potsdam.de
Deutsche Forschungsgemeinschaft (DFG) [EXC 314]; BMBF [03IS2201B]
Artavazd Badalyan
Meina Neumann-Schaal
Silke Leimkühler
Ursula Wollenberger
eng
uncontrolled
Aldehyde oxidoreductase
eng
uncontrolled
Benzaldehyde
eng
uncontrolled
Biosensor
eng
uncontrolled
Aromatic aldehydes
eng
uncontrolled
Molybdenum cofactor
Institut für Biochemie und Biologie
Referiert
37900
2014
2014
eng
3359
3364
6
14
406
article
Springer
Heidelberg
1
--
--
--
Characterization of the enhanced peroxidatic activity of amyloid beta peptide-hemin complexes towards neurotransmitters
Binding of heme to the amyloid peptides A beta 40/42 is thought to be an initial step in the development of symptoms in the early stages of Alzheimer's disease by enhancing the intrinsic peroxidatic activity of heme. We found considerably higher acceleration of the reaction for the physiologically relevant neurotransmitters dopamine and serotonin than reported earlier for the artificial substrate 3,3',5,5'-tetramethylbenzidine (TMB). Thus, the binding of hemin to A beta peptides might play an even more crucial role in the early stages of Alzheimer's disease than deduced from these earlier results. To mimic complex formation, a new surface architecture has been developed: The interaction between the truncated amyloid peptide A beta 1-16 and hemin immobilized on an aminohexanethiol spacer on a gold electrode has been analyzed by cyclic voltammetry. The resulting complex has a redox pair with a 25 mV more cathodic formal potential than hemin alone.
Analytical & bioanalytical chemistry
10.1007/s00216-014-7822-8
24760399
1618-2642
1618-2650
wos:2014
WOS:000336261800013
Scheller, F (reprint author), Fraunhofer Inst Biomed Engn IBMT, Muhlenberg 13, D-14476 Golm, Germany., fschell@uni-potsdam.de
BMBF of Germany [0311993]; Deutsche Forschungsgemeinschaft (DFG) [EXC 314]
Bettina Neumann
Aysu Yarman
Ursula Wollenberger
Frieder W. Scheller
eng
uncontrolled
Peroxidatic activity
Institut für Biochemie und Biologie
Referiert
35610
2012
2012
eng
71
77
7
5
87
article
Elsevier
Lausanne
1
--
--
--
Direct and mediated electrochemical response of the cytochrome P450 106A2 from Bacillus megaterium ATCC 13368
CYP106A2 is one of only a few known steroid hydroxylases of bacterial origin, which might be interesting for biotechnological applications. Despite the enzyme having been studied for more than 30 years, its physiological function remains elusive. To date, there have been no reports of the redox potential of CYP106A2, which was supposed to be unusually low for a cytochrome P450. In this work we show that cyclic voltammetry is not only suitable to determine the redox potential of challenging proteins such as CYP106A2, measured at - 128 mV vs. NHE, but also to study molecular interactions of the enzyme with different interaction partners via the respective electrochemical responses. The effect of small ligands, such as carbon monoxide and cyanide, was observed on the cyclic voltammograms of CYP106A2. Furthermore, we found that Tween 80 caused a positive shift of the redox potential of immobilised CYP106A2 indicative for water expulsion from the haem environment. Moreover, electron transfer mediation phenomena with biological redox partners (e.g. ferredoxins) were studied. Finally, the influence of two different kinds of substrates on the electrochemical response of CYP106A2 was assessed, aligning observations from spectral and electrochemical studies.
Bioelectrochemistry : an international journal devoted to electrochemical aspects of biology and biological aspects of electrochemistry ; official journal of the Bioelectrochemical Society
10.1016/j.bioelechem.2012.01.006
1567-5394
wos:2011-2013
WOS:000309033000012
de Oliveira, P (reprint author), Univ Paris 11, Fac Sci Orsay, Chim Phys Lab, CNRS,UMR 8000, Batiment 350, F-91405 Orsay, France., pedro.deoliveira@u-psud.fr
Centre Nationale de la Recherche Scientifique [UMR 8000]; Universite
Paris-Sud [11]; Unicat Cluster of Excellence (Deutsche
Forschungsgemeinschaft) [EXC314]
Helene Colas
Kerstin M. Ewen
Frank Hannemann
Nikitas Bistolas
Ursula Wollenberger
Rita Bernhardt
Pedro de Oliveira
eng
uncontrolled
Cytochrome P450
eng
uncontrolled
Cyclic voltammetry
eng
uncontrolled
Modified electrode
eng
uncontrolled
Protein interaction
eng
uncontrolled
Substrate binding
Institut für Biochemie und Biologie
Referiert
36389
2012
2012
eng
405
412
8
1
402
article
Springer
Heidelberg
1
--
--
--
The aromatic peroxygenase from Marasmius rutola-a new enzyme for biosensor applications
The aromatic peroxygenase (APO; EC 1.11.2.1) from the agraric basidomycete Marasmius rotula (MroAPO) immobilized at the chitosan-capped gold-nanoparticle-modified glassy carbon electrode displayed a pair of redox peaks with a midpoint potential of -278.5 mV vs. AgCl/AgCl (1 M KCl) for the Fe(2+)/Fe(3+) redox couple of the heme-thiolate-containing protein. MroAPO oxidizes aromatic substrates such as aniline, p-aminophenol, hydroquinone, resorcinol, catechol, and paracetamol by means of hydrogen peroxide. The substrate spectrum overlaps with those of cytochrome P450s and plant peroxidases which are relevant in environmental analysis and drug monitoring. In M. rotula peroxygenase-based enzyme electrodes, the signal is generated by the reduction of electrode-active reaction products (e.g., p-benzoquinone and p-quinoneimine) with electro-enzymatic recycling of the analyte. In these enzyme electrodes, the signal reflects the conversion of all substrates thus representing an overall parameter in complex media. The performance of these sensors and their further development are discussed.
Analytical & bioanalytical chemistry
10.1007/s00216-011-5497-y
1618-2642
wos:2011-2013
WOS:000298749300044
Scheller, FW (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25, D-14476 Golm, Germany., fschell@uni-potsdam.de
BMBF of Germany [0311993]; Deutsche Forschungsgemeinschaft within German Excellence Initiative [EXC 314)]
Aysu Yarman
Glenn Gröbe
Bettina Neumann
Mathias Kinne
Nenad Gajovic-Eichelmann
Ursula Wollenberger
Martin Hofrichter
Rene Ullrich
Katrin Scheibner
Frieder W. Scheller
eng
uncontrolled
Unspecific peroxygenase
eng
uncontrolled
Cytochrome P450
eng
uncontrolled
Biosensors
eng
uncontrolled
Phenolic substances
Institut für Biochemie und Biologie
Referiert
36354
2012
2012
eng
4615
4618
4
11
22
article
Royal Society of Chemistry
Cambridge
1
--
--
--
Semimetallic TiO2 nanotubes new interfaces for bioelectrochemical enzymatic catalysis
Different self-organized TiO2 nanotube structures are shown to represent new interfaces for the achievement of bioelectrochemical enzymatic catalysis involving redox proteins and enzymes without further surface modification or the presence of mediators.
Journal of materials chemistry
10.1039/c2jm16427b
0959-9428
wos:2011-2013
WOS:000300571400009
Lisdat, F (reprint author), Wildau Univ Appl Sci, Bahnhofstr 1, D-15745 Wildau, Germany., flisdat@th-wildau.de
BMBF, Germany [03IS2201I]
David Sarauli
Marc Riedel
Christoph Wettstein
Robert Hahn
Konstanze Stiba
Ursula Wollenberger
Silke Leimkühler
Patrik Schmuki
Fred Lisdat
Institut für Biochemie und Biologie
Referiert
45320
2016
2016
eng
24
30
7
109
article
Elsevier
Lausanne
1
--
--
--
Wiring of the aldehyde oxidoreductase PaoABC to electrode surfaces via entrapment in low potential phenothiazine-modified redox polymers
Phenothiazine-modified redox hydrogels were synthesized and used for the wiring of the aldehyde oxidoreductase PaoABC to electrode surfaces. The effects of the pH value and electrode surface modification on the biocatalytic activity of the layers were studied in the presence of vanillin as the substrate. The enzyme electrodes were successfully employed as bioanodes in vanillin/O-2 biofuel cells in combination with a high potential bilirubin oxidase biocathode. Open circuit voltages of around 700 mV could be obtained in a two compartment biofuel cell setup. Moreover, the use of a rather hydrophobic polymer with a high degree of crosslinking sites ensures the formation of stable polymer/enzyme films which were successfully used as bioanode in membrane-less biofuel cells. (C) 2015 Elsevier B.V. All rights reserved.
Bioelectrochemistry : an international journal devoted to electrochemical aspects of biology and biological aspects of electrochemistry ; official journal of the Bioelectrochemical Society
10.1016/j.bioelechem.2015.12.005
26775204
1567-5394
1878-562X
wos2016:2019
WOS:000373418400003
Schuhmann, W (reprint author), Ruhr Univ Bochum, Analyt Chem, CES, Univ Str 150, D-44780 Bochum, Germany., wolfgang.schuhmann@ruhr-uni-bochum.de
Deutsche Forschungsgemeinschaft [EXC 1069, EXC 314]; BMBF [03IS2201F]; Deutscher Akademischer Austauschdienst (DAAD)
importub
2020-03-22T17:33:01+00:00
filename=package.tar
0ef1373d9e79d162b7ab892b514d7243
Piyanut Pinyou
Adrian Ruff
Sascha Poeller
Sabine Alsaoub
Silke Leimkühler
Ursula Wollenberger
Wolfgang Schuhmann
eng
uncontrolled
Aldehyde oxidoreductase
eng
uncontrolled
Enzyme electrode
eng
uncontrolled
Redox polymer
eng
uncontrolled
Phenothiazine
eng
uncontrolled
Biosensor
eng
uncontrolled
Biofuel cell
Institut für Biochemie und Biologie
Referiert
Import
44885
2016
2016
eng
2303
2310
8
28
article
Wiley-VCH
Weinheim
1
--
--
--
Role of Conductive Nanoparticles in the Direct Unmediated Bioelectrocatalysis of Immobilized Sulfite Oxidase
Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
10.1002/elan.201600246
1040-0397
1521-4109
wos2016:2019
WOS:000387886500007
Wollenberger, U (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25,Haus 25, D-14476 Golm, Germany., uwollen@uni-potsdam.de
Unicat Cluster of Excellence - Deutsche Forschungsgemeinschaft [EXC 314/2]
importub
2020-03-22T13:55:01+00:00
filename=package.tar
b4a56b40b2975747172d06e6aecbc437
Ting Zeng
Stefano Frasca
Jens Rumschöttel
Joachim Koetz
Silke Leimkühler
Ursula Wollenberger
eng
uncontrolled
Direct electron transfer
eng
uncontrolled
Protein voltammetry
eng
uncontrolled
Human sulfite oxidase
eng
uncontrolled
Bioelectrocatalysis
eng
uncontrolled
Nanoparticles
Institut für Chemie
Institut für Biochemie und Biologie
Referiert
Import
44886
2016
2016
eng
2400
2407
8
28
article
Wiley-VCH
Weinheim
1
--
--
--
Electrogeneration of O-2(center dot-) and H2O2 Using Polymer-modified Microelectrodes in the Environment of Living Cells
Microelectrodes modified with electropolymerized plumbagin (PLG) were used for the generation of superoxide radical (O-2(center dot-)) and hydrogen peroxide (H2O2) during oxygen reduction reaction (ORR) in an aqueous medium, specifically in serum-free cell culture media. This is enabled by the specific design of a polymer film on the microelectrode. The generation and diffusion of O-2(center dot-) during electrocatalytic ORR at a positionable PLG polymer-modified microelectrode was followed by fluorescence microscopy with the selective dye 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl) and by amperometric detection using a cytochrome c-modified electrode at + 0.13 V. H2O2 production, either by direct oxygen reduction or as product of O-2(center dot-) disproportionation, was monitored by the reaction with Amplex UltraRed. The PLG polymer-modified microelectrodes were used to expose mammalian B6-RPE07 retinal cells to defined local fluxes of reactive oxygen species (ROS), and cellular responses and morphological alterations were observed. The use of a controllable source of ROS opens many possibilities to study how living cells respond to the presence of a certain flux of specific ROS.
Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
10.1002/elan.201600267
1040-0397
1521-4109
wos2016:2019
WOS:000387886500019
Wittstock, G (reprint author), Carl von Ossietzky Univ Oldenburg, Fac Math & Sci, Inst Chem, D-26111 Oldenburg, Germany., gunther.wittstock@uni-oldenburg.de
German Academic Exchange Service (DAAD) [A/12/90549]; Deutsche Forschungsgemeinschaft (RTG) [1885/1]
importub
2020-03-22T13:55:01+00:00
filename=package.tar
b4a56b40b2975747172d06e6aecbc437
Saustin Dongmo
Janina Leyk
Carsten Dosche
Christiane Richter-Landsberg
Ursula Wollenberger
Gunther Wittstock
eng
uncontrolled
reactive oxygen species
eng
uncontrolled
microelectrode
eng
uncontrolled
scanning electrochemical microscopy
eng
uncontrolled
biosensor
eng
uncontrolled
polymer-modified electrode
eng
uncontrolled
oxygen reduction reaction
Institut für Biochemie und Biologie
Referiert
Import
45221
2016
2016
eng
6382
6389
8
88
article
American Chemical Society
Washington
1
--
--
--
Interaction of Flavin-Dependent Fructose Dehydrogenase with Cytochrome c as Basis for the Construction of Biomacromolecular Architectures on Electrodes
The creation of electron transfer (ET) chains based on the defined arrangement of enzymes and redox proteins on electrode surfaces represents an interesting approach within the field of bioelectrocatalysis. In this study, we investigated the ET reaction of the flavin-dependent enzyme fructose dehydrogenase (FDH) with the redox protein cytochrome c (cyt c). Two different pH optima were found for the reaction in acidic and neutral solutions. When cyt c was adsorbed on an electrode surface while the enzyme remained in solution, ET proceeded efficiently in media of neutral pH. Interprotein ET was also observed in acidic media; however, it appeared to be less efficient. These findings suggest that two different ET pathways between the enzyme and cyt c may occur. Moreover, cyt c and FDH were immobilized in multiple layers on an electrode surface by means of another biomacromolecule: DNA (double stranded) using the layer -by -layer technique. The biprotein multilayer architecture showed a catalytic response in dependence on the fructose concentration, indicating that the ET reaction between both proteins is feasible even in the immobilized state. The electrode showed a defined response to fructose and a good storage stability. Our results contribute to the better understanding of the ET reaction between FDH and cyt c and provide the basis for the creation of all-biomolecule based fructose sensors the sensitivity of which can be controlled by the layer preparation.
Analytical chemistry
10.1021/acs.analchem.6b00815
27213223
0003-2700
1520-6882
wos2016:2019
WOS:000378470200042
Lisdat, F (reprint author), Tech Univ Appl Sci Wildau, Inst Appl Life Sci, Biosyst Technol, Hsch Ring 1, D-15745 Wildau, Germany., fred.lisdat@th-wildau.de
DFG [Li 706/7-1]
importub
2020-03-22T16:43:01+00:00
filename=package.tar
a35c91e9f97d5abe174cb3755ab9274a
Christoph Wettstein
Kenji Kano
Daniel Schaefer
Ursula Wollenberger
Fred Lisdat
Institut für Biochemie und Biologie
Referiert
Import
45688
2016
2016
eng
375
382
8
75
article
Elsevier
Oxford
1
--
--
--
Prediction of wastewater quality using amperometric bioelectronic tongues
Wastewater samples from a Swedish chemi-thermo-mechanical pulp (CTMP) mill collected at different purification stages in a wastewater treatment plant (WWTP) were analyzed with an amperometric enzyme-based biosensor array in a flow-injection system. In order to resolve the complex composition of the wastewater, the array consists of several sensing elements which yield a multidimensional response. We used principal component analysis (PCA) to decompose the array's responses, and found that wastewater with different degrees of pollution can be differentiated. With the help of partial least squares regression (PLS-R), we could link the sensor responses to the toxicity parameter, as well as to global organic pollution parameters (COD, BOD, and TOC). From investigating the influences of individual sensors in the array, it was found that the best models were in most cases obtained when all sensors in the array were included in the PLS-R model. We find that fast simultaneous determination of several global environmental parameters characterizing wastewaters is possible with this kind of biosensor array, in particular because of the link between the sensor responses and the biological effect onto the ecosystem into which the wastewater would be released. In conjunction with multivariate data analysis tools, there is strong potential to reduce the total time until a result is yielded from days to a few minutes.
Marine policy
10.1016/j.bios.2015.08.055
26342573
0956-5663
1873-4235
wos2016:2019
WOS:000362862000049
Czolkos, I (reprint author), Tech Univ Denmark, DTU Nanotech Dept Micro & Nanotechnol, 2800 Kgs, DK-2800 Lyngby, Denmark., ilcz@nanotech.dtu.dk; ilcz@nanotech.dtu.dk
European Commission [IntelliSens: QLK3-2000-01481]; Swedish Research Council (Vetenskapsradet)
importub
2020-03-22T20:37:01+00:00
filename=package.tar
332feeb102b398577d86ab5a0b234af7
Ilja Czolkos
Eva Dock
Erik Tonning
Jakob Christensen
Margrethe Winther-Nielsen
Charlotte Carlsson
Renata Mojzikova
Petr Skladal
Ursula Wollenberger
Lars Norgaard
Tautgirdas Ruzgas
Jenny Emneus
eng
uncontrolled
Biosensor array
eng
uncontrolled
Electronic tongue
eng
uncontrolled
Amperometric sensor
eng
uncontrolled
Screen-printed electrode
eng
uncontrolled
Multivariate data analysis
eng
uncontrolled
Chemometrics
eng
uncontrolled
Wastewater
eng
uncontrolled
Toxicity
eng
uncontrolled
Phenolic compounds
Institut für Biochemie und Biologie
Referiert
Import
45876
2016
2016
eng
579
587
9
408
article
Springer
Heidelberg
1
--
--
--
Mediated bioelectrochemical system for biosensing the cell viability of Staphylococcus aureus
Staphylococcus aureus is one of the most dangerous human pathogens and is the cause of numerous illnesses ranging from moderate skin infections to life-threatening diseases. Despite advances made in identifying microorganisms, rapid detection methods for the viability of bacteria are still missing. Here, we report a rapid electrochemical assay for cell viability combining the use of double redox mediators and multiwall carbon nanotubes-screen printed electrodes (MWCNTs-SPE), ferricyanide (FCN) and 2,6-dichlorophenolindophenol (DCIP), which served as electron shuttle to enable the bacterial-electrode communications. The current originating from the metabolically active cells was recorded for probing the activity of the intracellular redox centers. Blocking of the respiratory chain pathways with electron transfer inhibitors demonstrated the involvement of the electron transport chain in the reaction. A good correlation between the number of the metabolically active cells and the current was obtained. The proposed assay has been exploited for monitoring cell proliferation of S. aureus during the growth. The sensitivity of the detection method reached 0.1 OD600. Therefore, the technique described is promising for estimating the cell number, measuring the cell viability, and probing intracellular redox center(s).
Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry and Analusis
10.1007/s00216-015-9134-z
26522330
1618-2642
1618-2650
wos2016:2019
WOS:000368016400023
Hassan, RYA (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknechtstr 24-25, D-14476 Potsdam, Germany., rabeayy@yahoo.com
Egyptian Ministry of Higher Education and Scientific Research; German Academic Exchange Service (DAAD); Taschentuchlabor IZIB - BMBF [03IS2201B]
importub
2020-03-22T22:11:01+00:00
filename=package.tar
05533e171e9f777aab1012709f66d2b4
Rabeay Y. A. Hassan
Ursula Wollenberger
eng
uncontrolled
Microbial electrochemistry
eng
uncontrolled
Pathogenic detection
eng
uncontrolled
Probing living Staphylococcus aureus
eng
uncontrolled
CNTs-based screen printed electrodes
Institut für Biochemie und Biologie
Referiert
Import
46055
2006
2006
eng
2324
2330
7
23
18
article
Wiley-VCH
Weinheim
1
2006-11-27
2006-11-27
--
Influence of modifications on the efficiency of pyrolysed CoTMPP as electrode material for horseradish peroxidase and the reduction of hydrogen peroxide
A tailor-made horseradish peroxidase (HRP) bulk composite electrode was developed on the basis of pyrolyzed cobalt tetramethoxyphenylporphyrin (CoTMPP) by modifying pore size and surface area of the porous carbon material through varying amounts of iron oxalate and sulfur prior to pyrolyzation. The materials were used to immobilize horseradish peroxidase (HRP). These electrodes were characterized in terms of their efficiency to reduce hydrogen peroxide. The heterogeneous electron transfer rate constants of different materials were determined with the rotating disk electrode method and a k(S) (401 +/- 61 s(-1)) exceeding previously reported values for native HRP was found.
Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
10.1002/elan.200603664
1040-0397
wos:2006
WOS:000242689900006
Katterle, M (reprint author), Univ Potsdam, Inst Biochem & Biol Analyt Biochem, Karl Liebknecht Str 24-25, D-14476 Golm, Germany., katterle@rz.uni-potsdam.de
importub
2020-04-16T08:41:35+00:00
filename=package.tar
5fa2a4142059f345449049ca463c7641
false
true
Noya Loew
Peter Bogdanoff
Iris Herrmann
Ursula Wollenberger
Frieder W. Scheller
Martin Katterle
eng
uncontrolled
cobalt porphyrin
eng
uncontrolled
electron transfer
eng
uncontrolled
horseradish peroxidase
eng
uncontrolled
hydrogen peroxide
eng
uncontrolled
immobilization
Biowissenschaften; Biologie
Institut für Biochemie und Biologie
Referiert
Import