TY - JOUR A1 - Scheller, Frieder W. A1 - Pfeiffer, Dorothea A1 - Schubert, Florian A1 - Wollenberger, Ursula T1 - Enzyme - based electrodes Y1 - 1995 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Lisdat, Fred A1 - Scheller, Frieder W. T1 - Enzymatic substrade recycling electrodes Y1 - 1997 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Schubert, Florian A1 - Pfeiffer, Dorothea A1 - Scheller, Frieder W. T1 - Enhancing biosensor performance using multienzyme systems Y1 - 1993 ER - TY - JOUR A1 - Neumann, Bettina A1 - Götz, Robert A1 - Wrzolek, Pierre A1 - Scheller, Frieder W. A1 - Weidinger, Inez M. A1 - Schwalbe, Matthias A1 - Wollenberger, Ulla T1 - Enhancement of the Electrocatalytic Activity of Thienyl-Substituted Iron Porphyrin Electropolymers by a Hangman Effect JF - ChemCatChem : heterogeneous & homogeneous & bio- & nano-catalysis ; a journal of ChemPubSoc Europe N2 - The thiophene-modified iron porphyrin FeT3ThP and the respective iron Hangman porphyrin FeH3ThP, incorporating a carboxylic acid hanging group in the second coordination sphere of the iron center, were electropolymerized on glassy carbon electrodes using 3,4-ethylenedioxythiophene (EDOT) as co-monomer. Scanning electron microscopy images and Resonance Raman spectra demonstrated incorporation of the porphyrin monomers into a fibrous polymer network. Porphyrin/polyEDOT films catalyzed the reduction of molecular oxygen in a four-electron reaction to water with onset potentials as high as +0.14V vs. Ag/AgCl in an aqueous solution of pH7. Further, FeT3ThP/polyEDOT films showed electrocatalytic activity towards reduction of hydrogen peroxide at highly positive potentials, which was significantly enhanced by introduction of the carboxylic acid hanging group in FeH3ThP. The second coordination sphere residue promotes formation of a highly oxidizing reaction intermediate, presumably via advantageous proton supply, as observed for peroxidases and catalases making FeH3ThP/polyEDOT films efficient mimics of heme enzymes. KW - activation of oxygen species KW - electro-polymerization KW - Hangman porphyrin KW - heterogeneous catalysis KW - immobilization Y1 - 2018 U6 - https://doi.org/10.1002/cctc.201800934 SN - 1867-3880 SN - 1867-3899 VL - 10 IS - 19 SP - 4353 EP - 4361 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Beissenhirtz, Moritz Karl A1 - Scheller, Frieder W. A1 - Viezzoli, Maria Silvia A1 - Lisdat, Fred T1 - Engineered superoxide dismutase monomers for superoxide biosensor applications N2 - Because of its high reaction rate and specificity, the enzyme superoxide dismutase (SOD) offers great potential for the sensitive quantification of superoxide radicals in electrochemical biosensors. In this work, monomeric mutants of human Cu,Zn-SOD were engineered to contain one or two additional cysteine residues, which could be used to bind the protein to gold surfaces, thus making the use of promotor molecules unnecessary. Six mutants were successfully designed, expressed, and purified. All mutants bound directly to unmodified gold surfaces via the sulfur of the cysteine residues and showed a quasireversible, direct electron transfer to the electrode. Thermodynamic and kinetic parameters of the electron transfer were characterized and showed only slight variations between the individual mutants. For one of the mutants, the interaction with the superoxide radical was studied in more detail. For both partial reactions of the dismutation, an interaction between protein and radical could be shown. In an amperometric biosensorial approach, the SOD-mutant electrode was successfully applied for the detection of superoxide radicals. In the oxidation region, the electrode surpassed the sensitivity of the commonly used cytochrome c electrodes by similar to 1 order of magnitude while not being limited by interferences, but the electrode did not fully reach the sensitivity of dimeric Cu,Zn-SOD immobilized on MPA-modified gold Y1 - 2006 UR - http://pubs.acs.org/journal/ancham U6 - https://doi.org/10.1021/Ac051465g SN - 0003-2700 ER - TY - JOUR A1 - Kirstein, Dieter A1 - Kirstein, Lincoln A1 - Scheller, Frieder W. A1 - Dieckmann, St. A1 - Ronnenberg, J. A1 - Beckmann, Dieter A1 - Weckenbrock, E. T1 - Elektroenzymatische Reduktion von Nitrat Y1 - 1994 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Bistolas, Nikitas A1 - Jung, Christiane A1 - Shumyantseva, V. V. A1 - Ruzgas, T. A1 - Scheller, Frieder W. T1 - Elektroden-Design für elektronische Wechselwirkung mit Monooxygenasen Y1 - 2004 SN - 3-8047-2132-x ER - TY - JOUR A1 - Stojanovic, Zorica A1 - Erdossy, Julia A1 - Keltai, Katalin A1 - Scheller, Frieder W. A1 - Gyurcsanyi, Robert E. T1 - Electrosynthesized molecularly imprinted polyscopoletin nanofilms for human serum albumin detection JF - Analytica chimica acta : an international journal devoted to all branches of analytical chemistry N2 - Molecularly imprinted polymers (MIPs) rendered selective solely by the imprinting with protein templates lacking of distinctive properties to facilitate strong target-MIP interaction are likely to exhibit medium to low template binding affinities. While this prohibits the use of such MIPs for applications requiring the assessment of very low template concentrations, their implementation for the quantification of high-abundance proteins seems to have a clear niche in the analytical practice. We investigated this opportunity by developing a polyscopoletin-based MIP nanofilm for the electrochemical determination of elevated human serum albumin (HSA) in urine. As reference for a low abundance protein ferritin-MIPs were also prepared by the same procedure. Under optimal conditions, the imprinted sensors gave a linear response to HSA in the concentration range of 20-100 mg/dm(3), and to ferritin in the range of 120-360 mg/dm(3). While as expected the obtained limit of detection was not sufficient to determine endogenous ferritin in plasma, the HSA-sensor was successfully employed to analyse urine samples of patients with albuminuria. The results suggest that MIP-based sensors may be applicable for quantifying high abundance proteins in a clinical setting. (c) 2017 Elsevier B.V. All rights reserved. KW - Human serum albumin KW - Ferritin KW - Molecularly imprinted polymer KW - Scopoletin KW - Urine Y1 - 2017 U6 - https://doi.org/10.1016/j.aca.2017.04.043 SN - 0003-2670 SN - 1873-4324 VL - 977 SP - 1 EP - 9 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Zhang, Xiaorong A1 - Yarman, Aysu A1 - Erdossy, Julia A1 - Katz, Sagie A1 - Zebger, Ingo A1 - Jetzschmann, Katharina J. A1 - Altintas, Zeynep A1 - Wollenberger, Ulla A1 - Gyurcsanyi, Robert E. A1 - Scheller, Frieder W. T1 - Electrosynthesized MIPs for transferrin BT - Plastibodies or nano-filters? JF - Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics N2 - Molecularly imprinted polymer (MP) nanofilrns for transferrin (Trf) have been synthesized on gold surfaces by electro-polymerizing the functional monomer scopoletin in the presence of the protein target or around pre-adsorbed Trf. As determined by atomic force microscopy (AFM) the film thickness was comparable with the molecular dimension of the target. The target (re)binding properties of the electro-synthesized MIP films was evaluated by cyclic voltammetry (CV) and square wave voltammetry (SWV) through the target-binding induced permeability changes of the MIP nanofilms to the ferricyanide redox marker, as well as by surface plasmon resonance (SPR) and surface enhanced infrared absorption spectroscopy (SEIRAS) of the immobilized protein molecules. For Trf a linear concentration dependence in the lower micromolar range and an imprinting factor of similar to 5 was obtained by SWV and SPR. Furthermore, non-target proteins including the iron-free apo-Trf were discriminated by pronounced size and shape specificity. Whilst it is generally assumed that the rebinding of the target or of cross-reacting proteins exclusively takes place at the polymer here we considered also the interaction of the protein molecules with the underlying gold transducers. We demonstrate by SWV that adsorption of proteins suppresses the signal of the redox marker even at the bare gold surface and by SEIRAS that the treatment of the MIP with proteinase K or NaOH only partially removes the target protein. Therefore, we conclude that when interpreting binding of proteins to directly MIP-covered gold electrodes the interactions between the protein and the gold surface should also be considered. KW - Molecularly imprinted polymer KW - Scopoletin KW - Transferrin KW - Protein adsorption KW - Redox marker Y1 - 2018 U6 - https://doi.org/10.1016/j.bios.2018.01.011 SN - 0956-5663 SN - 1873-4235 VL - 105 SP - 29 EP - 35 PB - Elsevier CY - Oxford ER - TY - JOUR A1 - Lei, Chenghong A1 - Wollenberger, Ursula A1 - Bistolas, Nikitas A1 - Guiseppi-Eli, A. A1 - Scheller, Frieder W. T1 - Electron transfer of hemoglobin at electrodes modified with colloidal clay nanoparticles Y1 - 2002 ER - TY - JOUR A1 - Ge, Bixia A1 - Scheller, Frieder W. A1 - Lisdat, Fred T1 - Electrochemistry of immobilized CuZnSOD and FeSOD and their interaction with superoxide radicals N2 - Copper, zinc superoxide dismutase (CuZnSOD) from bovine erythrocytes and iron superoxide dismutase from Escherichia coli (FeSOD) were immobilized on 3-mercaptopropionic acid (MPA)-modified gold electrodes, respectively. The characterization of the SOD electrodes showed a quasi-reversible, electrochemical redox behavior with a formal potential of 47 ñ 4 mV and -154 ñ 5 mV (vs. Ag/AgCl, 1 M KCl) for surface adsorbed CuZnSOD and FeSOD, respectively. The heterogeneous electron transfer rate constants were determined to be about 65 and 35/s, respectively. Covalent fixation of both SODs was also feasible with only slight changes in the formal potential. The interaction of superoxide radicals (O2-) with the SOD electrode was investigated. No catalytic current could be observed. However, due to the fast cyclic reaction of SOD with superoxide, the communication of the protein with the electrode was strongly influenced. The amperometric detection of superoxide radicals is discussed. Y1 - 2003 ER - TY - JOUR A1 - Katterle, Martin A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Electrochemistry of hemoglobin at modified silver electrodes is not a redox-process of iron protoporhyrin IX Y1 - 1997 ER - TY - JOUR A1 - Ju, Huangxian A1 - Liu, Songqin A1 - Ge, Bixia A1 - Lisdat, Fred A1 - Scheller, Frieder W. T1 - Electrochemistry of cytochrome c immobilized on colloidal gold modified carbon paste electrodes and its electrocatalytic activity Y1 - 2000 ER - TY - JOUR A1 - Pfeiffer, Dorothea A1 - Schubert, Frank A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Electrochemical sensors : enzyme electrodes and field effect transistors Y1 - 1996 ER - TY - JOUR A1 - Welzel, H.-P. A1 - Kossmehl, G. A1 - Engelmann, G. A1 - Neumann, B. A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Electrochemical polymerization of functionalized thiohene derivatives for immobilization of proteins Y1 - 1997 ER - TY - JOUR A1 - Kulys, J. A1 - Krikstopaitis, K. A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Electrochemical parameters of phenoxazine derivatives in solution and at monolayer-modified gold electrodes N2 - 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 Y1 - 2004 ER - TY - JOUR A1 - Ozcelikay, Goksu A1 - Kurbanoglu, Sevinc A1 - Zhang, Xiaorong A1 - Söz, Çağla Kosak A1 - Wollenberger, Ulla A1 - Ozkan, Sibel A. A1 - Yarman, Aysu A1 - Scheller, Frieder W. T1 - Electrochemical MIP Sensor for Butyrylcholinesterase JF - Polymers N2 - Molecularly imprinted polymers (MIPs) mimic the binding sites of antibodies by substituting the amino acid-scaffold of proteins by synthetic polymers. In this work, the first MIP for the recognition of the diagnostically relevant enzyme butyrylcholinesterase (BuChE) is presented. The MIP was prepared using electropolymerization of the functional monomer o-phenylenediamine and was deposited as a thin film on a glassy carbon electrode by oxidative potentiodynamic polymerization. Rebinding and removal of the template were detected by cyclic voltammetry using ferricyanide as a redox marker. Furthermore, the enzymatic activity of BuChE rebound to the MIP was measured via the anodic oxidation of thiocholine, the reaction product of butyrylthiocholine. The response was linear between 50 pM and 2 nM concentrations of BuChE with a detection limit of 14.7 pM. In addition to the high sensitivity for BuChE, the sensor responded towards pseudo-irreversible inhibitors in the lower mM range. KW - molecularly imprinted polymers KW - biomimetic sensors KW - butyrylcholinesterase KW - o-phenylenediamine KW - rivastigmine Y1 - 2019 U6 - https://doi.org/10.3390/polym11121970 SN - 2073-4360 VL - 11 IS - 12 PB - MDPI CY - Basel ER - TY - JOUR A1 - Jin, Wen A1 - Wollenberger, Ursula A1 - Kärgel, E. A1 - Schunck, W.-H. A1 - Scheller, Frieder W. T1 - Electrochemical investigation of the intermolecular electron transfer between cytochrome c and NADPH-cytochrome P450-reductase Y1 - 1997 ER - TY - JOUR A1 - Fridman, Vadim A1 - Wollenberger, Ursula A1 - Bogdanovskaya, V. A. A1 - Lisdat, Fred A1 - Ruzgas, T. A1 - Lindgren, A. A1 - Gorton, Lo A1 - Scheller, Frieder W. T1 - Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator Y1 - 2000 ER - TY - JOUR A1 - Warsinke, Axel A1 - Benkert, Alexander A1 - Scheller, Frieder W. T1 - Electrochemical immunoassays Y1 - 2000 ER - TY - JOUR A1 - Dechtrirat, Decha A1 - Gajovic-Eichelmann, Nenad A1 - Wojcik, Felix A1 - Hartmann, Laura A1 - Bier, Frank Fabian A1 - Scheller, Frieder W. T1 - Electrochemical displacement sensor based on ferrocene boronic acid tracer and immobilized glycan for saccharide binding proteins and E. coli JF - Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics N2 - Pathogens such as viruses and bacteria use their envelope proteins and their adhesin lectins to recognize the glycan residues presented on the cell surface of the target tissues. This principle of recognition is used in a new electrochemical displacement sensor for the protein concanavalin A (ConA). A gold electrode was first modified with a self-assembled monolayer of a thiolated mannose/OEG conjugate and a ferrocene boroxol derivative was pre-assembled as reporter molecule onto the mannose surface. The novel tracer molecule based on a 2-hydroxymethyl phenyl boronic acid derivative binds even at neutral pH to the saccharides which could expand the application towards biological samples (i.e., urine and feces). Upon the binding of ConA, the tracer was displaced and washed away from the sensor surface leading to a decrease in the electrochemical signal. Using square wave voltammetry (SWV), the concentration of ConA in the sample solution could be determined in the dynamic concentration range established from 38 nmol L-1 to 5.76 mu mol L-1 with a reproducible detection limit of 1 mu g mL(-1) (38 nmol L-1) based on the signal-to-noise ratio (S/N=3) with fast response of 15 min. The new reporter molecule showed a reduced non-specific displacement by BSA and ribonuclease A. The sensor was also successfully transferred to the first proof of principle for the detection of Escherichia coli exhibiting a detection limit of approximately 6 x 102 cells/mL Specificity of the displacement by target protein ConA and E. coli was demonstrated since the control proteins (i.e., BSA and RNaseA) and the control E. coli strain, which lack of type 1 fimbriae, were ineffective. (C) 2014 Elsevier B.V. All rights reserved. KW - Ferrocene benzoboroxol biosensor KW - Concanavalin A KW - Displacement KW - Escherichia coli KW - Ferrocene boronic acid KW - Self-assembled monolayer Y1 - 2014 U6 - https://doi.org/10.1016/j.bios.2014.02.028 SN - 0956-5663 SN - 1873-4235 VL - 58 SP - 1 EP - 8 PB - Elsevier CY - Oxford ER - TY - JOUR A1 - Chen, Jian A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Electrochemical determination of human hemoglobin by using ferrocene carboxylic acid modified carbon powder microelectrode Y1 - 2003 ER - TY - JOUR A1 - Mak, Wing Cheung A1 - Cheung, Kwan Yee A1 - Trau, Dieter A1 - Warsinke, Axel A1 - Scheller, Frieder W. A1 - Renneberg, Reinhard T1 - Electrochemical bioassay utilizing encapsulated electrochemical active microcrystal biolabels N2 - A new approach to perform electrochemical immunoassay based on the utilization of encapsulated microcrystal was developed. The microcrystal labels create a "supernova effect" upon exposure to a desired releasing agent. The microcrystal cores dissolve, and large amounts of signal-generating molecules diffuse across the capsule wall into the outer environment. Layer-by-Layer (LbL) technology was employed for the encapsulation of electrochemical signal- generating microcrystals (ferrocene microcrystals). The encapsulated microcrystals were conjugated with antibody molecules through the adsorption process. The biofunctionalized microcrystals were utilized as a probe for immunoassays. The microcrystal-based label system provided a high-signal molecule to antibody (SIP) ratio of 10(4)-10(5). Microcrystal biolabels with different antibody surface coverage (1.60-5.05 mg m(-2)) were subjected to a solid-phase immunoassay for the detection of mouse immunoglobulin G (M-IgG) molecules. The microcrystal-based immunoassay for the detection of M-IgG performed with microcrystals having antibody surface coverage of 5.05 mg m(-2) showed a sensitivity of 3.93 nA g(- 1) L-1 with a detection limit of 2.82 g L-1 Y1 - 2005 SN - 0003-2700 ER - TY - JOUR A1 - Lisdat, Fred A1 - Ge, Bixia A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. A1 - Meyer, T. T1 - Electrochemical behaviour and nitric oxides interaction of immobilised cytochrome c from Rhodocyclus gelatinosus Y1 - 2000 ER - TY - JOUR A1 - Kapp, Andreas A1 - Beissenhirtz, Moritz Karl A1 - Geyer, F. A1 - Scheller, Frieder W. A1 - Viezzoli, Maria Silvia A1 - Lisdat, Fred T1 - Electrochemical and sensorial behaviour of SOD mutants immobilized on gold electrodes in aqueous / organic solvent mixtures Y1 - 2006 UR - http://www3.interscience.wiley.com/cgi-bin/jhome/26571/ U6 - https://doi.org/10.1002/elan.200603620 SN - 1040-0397 ER - TY - JOUR A1 - Spricigo, Roberto A1 - Dronov, Roman A1 - Lisdat, Fred A1 - Leimkühler, Silke A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer N2 - 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. Y1 - 2009 UR - http://www.springerlink.com/content/100417 U6 - https://doi.org/10.1007/s00216-008-2432-y SN - 1618-2642 ER - TY - JOUR A1 - Kulys, J. A1 - Drungiliene, A. A1 - Wollenberger, Ursula A1 - Krikstopaitis, K. A1 - Scheller, Frieder W. T1 - Electroanalytical determination of peroxidases and laccases on carbon paste electrodes Y1 - 1997 ER - TY - JOUR A1 - Beissenhirtz, Moritz Karl A1 - Scheller, Frieder W. A1 - Stöcklein, Walter F. M. A1 - Kurth, D. A1 - Möhwald, Helmuth A1 - Lisdat, Fred T1 - Electroactive cytochrome c multilayers within a polyelectrolyte assembly Y1 - 2004 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. T1 - Einsatz von Enzymen und Antikörpern in organischen Lösungsmitteln Y1 - 1995 ER - TY - JOUR A1 - Makower, Alexander A1 - Barmin, Anatoli V. A1 - Scheller, Frieder W. T1 - Eine neue Methode zur hochempfindlichen Analyse von Pestiziden Y1 - 2000 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. A1 - Abuknesha, Rhamadan T1 - Effects of organic solvents on semicontinuous immunochemical detection of coumarin derivatives Y1 - 1995 ER - TY - JOUR A1 - Paeschke, Manfred A1 - Hintsche, Rainer A1 - Wollenberger, Ursula A1 - Jin, Wen A1 - Scheller, Frieder W. T1 - Dynamic redox recycling of cytochrome c Y1 - 1995 SN - 0022-0728 ER - TY - JOUR A1 - Shumyantseva, V. V. A1 - Ivanov, Y. D. A1 - Bistolas, Nikitas A1 - Scheller, Frieder W. A1 - Archakov, Alexander I. A1 - Wollenberger, Ursula T1 - Direct electron transfer of cytochrome P450 2B4 at electrodes modified with non-ionic detergent and colloidal clay nanoparticles N2 - 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 Y1 - 2004 ER - TY - JOUR A1 - Wu, Yunhua A1 - Wollenberger, Ursula A1 - Hofrichter, Martin A1 - Ullrich, Rene A1 - Scheibner, Katrin A1 - Scheller, Frieder W. T1 - Direct electron transfer of Agrocybe aegerita peroxygenase at electrodes modified with chitosan-capped Au nanoparticles and its bioelectrocatalysis to aniline JF - Sensors and actuators : B, Chemical N2 - 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. KW - Agrocybe aegerita peroxygenase KW - Au nanoparticles KW - Direct electron transfer KW - Aniline biosensor KW - Bioelectrocatalysis Y1 - 2011 U6 - https://doi.org/10.1016/j.snb.2011.09.090 SN - 0925-4005 VL - 160 IS - 1 SP - 1419 EP - 1426 PB - Elsevier CY - Lausanne ER - TY - JOUR A1 - Jin, Wen A1 - Bernhardt, Rita A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. T1 - Direct electron transfer of adrenodoxin-a [2Fe-2S] protein-- and its mutants on modified gold electrode Y1 - 1998 ER - TY - JOUR A1 - Tanne, Johannes A1 - Jeoung, Jae-Hun A1 - Peng, Lei A1 - Yarman, Aysu A1 - Dietzel, Birgit A1 - Schulz, Burkhard A1 - Schad, Daniel A1 - Dobbek, Holger A1 - Wollenberger, Ursula A1 - Bier, Frank Fabian A1 - Scheller, Frieder W. T1 - Direct Electron Transfer and Bioelectrocatalysis by a Hexameric, Heme Protein at Nanostructured Electrodes JF - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis N2 - A nanohybrid consisting of poly(3-aminobenzenesulfonic acid-co-aniline) and multiwalled carbon nanotubes [MWCNT-P(ABS-A)]) on a gold electrode was used to immobilize the hexameric tyrosine-coordinated heme protein (HTHP). The enzyme showed direct electron transfer between the heme group of the protein and the nanostructured surface. Desorption of the noncovalently bound heme from the protein could be excluded by control measurements with adsorbed hemin on aminohexanthiol-modified electrodes. The nanostructuring and the optimised charge characteristics resulted in a higher protein coverage as compared with MUA/MU modified electrodes. The adsorbed enzyme shows catalytic activity for the cathodic H2O2 reduction and oxidation of NADH. KW - HTHP KW - Nanohybrid KW - Poylaniline KW - Multiwalled carbon nanotube Y1 - 2015 U6 - https://doi.org/10.1002/elan.201500231 SN - 1040-0397 SN - 1521-4109 VL - 27 IS - 10 SP - 2262 EP - 2267 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Loew, Noya A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. A1 - Katterle, Martin T1 - Direct electrochemistry and spectroelectrochemistry of osmium substituted horseradish peroxidase N2 - 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. Y1 - 2009 UR - http://www.sciencedirect.com/science/journal/15675394 U6 - https://doi.org/10.1016/j.bioelechem.2009.03.015 SN - 1567-5394 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Drungiliene, A. A1 - Stöcklein, Walter F. M. A1 - Kulys, J. A1 - Scheller, Frieder W. T1 - Direct electrocatalytic determination of dissolved peroxidases Y1 - 1996 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Micheel, Burkhard A1 - Kempter, Gerhard A1 - Höhne, Wolfgang A1 - Scheller, Frieder W. T1 - Diphenylurea hapten sensing with a monoclonal antibody and its Fab fragment : kinetic and thermodynamic investigations Y1 - 1998 ER - TY - JOUR A1 - Halámek, Jan A1 - Wollenberger, Ursula A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. T1 - Development of a biosensor for glycated hemoglobin N2 - 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. Y1 - 2007 UR - http://www.sciencedirect.com/science/journal/00134686 U6 - https://doi.org/10.1016/j.electacta.2007.03.059 SN - 0013-4686 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Neumann, B. A1 - Scheller, Frieder W. T1 - Development of a biomimetic alkane sensor f Y1 - 1998 ER - TY - JOUR A1 - Scheller, Frieder W. T1 - Deutliche Signale setzen [Leitartikel] Y1 - 1999 ER - TY - JOUR A1 - Vijgenboom, E. A1 - Vijgenboom, E. A1 - Teppner, A. W. J. W. A1 - Makower, Alexander A1 - Scheller, Frieder W. A1 - Canters, Gerard W. A1 - Wollenberger, Ursula T1 - Determination of phenolic compounds using recombinant tyrosinanse from Streptomyces antibioticus Y1 - 2001 ER - TY - JOUR A1 - Ghindilis, A. L. A1 - Makower, Alexander A1 - Bauer, Christian G. A1 - Bier, Frank Fabian A1 - Scheller, Frieder W. T1 - Determination of p-aminophenol and catecholamines at picomolar concentrations based on recycling enzyme amplification Y1 - 1995 ER - TY - JOUR A1 - Ignatov, S. A1 - Ge, Bixia A1 - Scheller, Frieder W. A1 - Lisdat, Fred T1 - Detection of the antioxidant activity detection of flavonoids by using superoxide sensor Y1 - 2001 SN - 1-58603-164-3 ER - TY - JOUR A1 - Pieper-Fürst, U. A1 - Kleuser, U. A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Scheller, Frieder W. T1 - Detection of subicomolar concentrations of human matrix metalloproteinase-2 by an optical biosensor N2 - We describe in this paper the development of a one-step sandwich assay for the highly sensitive and fast detection of human matrix metalloproteinase (MMP)-2 (EC 3.4.24.24), using surface plasmon resonance (SPR). For the assay, two ligands were selected: monoclonal anti-MMP-2 antibody Ab-2 and the tissue inhibitor of metalloproteinases (TIMP)-2. They were chosen on the basis of (1) their affinities to MMP-2, (2) the efficiency of immobilization to the sensor chip, (3) the efficiency of adsorption to colloidal gold, and (4) the stability of these protein-coated gold particles. The assay included mixing of MMP-2 with antibody Ab-2 adsorbed to colloidal gold with a diameter of about 20 rim and injection into the flowcell of the SPR instrument containing immobilized TIMP-2. By using colloidal gold particles an amplification factor of 114 and a detection limit of 0.5 pM for MMP-2 were obtained. The precision of the assay was high even at low analyte concentrations, the standard deviation being 8.3% for five determinations of 1 pM MMP- 2. No significant binding was observed with the structurally related MMP-9. The assay is far more sensitive and faster than commonly used methods for MMP-2 detection. As TIMP-bound MMP-2 is not detected by this method, the assay can be applied for measuring free MMP-2, reflecting the imbalance of free and inhibitor-bound enzyme in various pathological situations. (C) 2004 Elsevier Inc. All rights reserved Y1 - 2004 ER - TY - JOUR A1 - Ehrentreich-Förster, Eva A1 - Scheller, Frieder W. A1 - Bier, Frank Fabian T1 - Detection of progesterone in whole blood samples N2 - The progesterone concentration in blood samples can be utilised as a marker for the diagnosis of early pregnancy, endocrinopathy and virilism. Here, we describe a method for progesterone detection and measurement in whole blood samples by a surface sensitive biosensor used in conjunction with an integrated optical grating coupler. This device determines refractive index changes near the biosensor's surface. Hence, biological species bound to a surface layer can be measured in real-time without any label. For the measurements, we have modified the indirect competitive immonoassay principle. The concentration of the progesterone antibody was kept at 1 µg/ml. Progesterone concentration was determined in buffer solution and whole blood in a range between 0.005 and 10 ng/ml. The detection limit was determined to be 3 pM. The relative standard deviation was calculated to be 3.5%. Y1 - 2003 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Micheel, Burkhard A1 - Höhne, Wolfgang A1 - Woller, Jochen A1 - Kempter, Gerhard A1 - Scheller, Frieder W. T1 - Detection of diphenylurea derivatives with biospecific interaction analysis (BIA) : Kinetic investigations Y1 - 1997 ER - TY - JOUR A1 - Bistolas, Nikitas A1 - Wollenberger, Ursula A1 - Jung, Christiane A1 - Scheller, Frieder W. T1 - Cytochrome P450 biosensors : a review N2 - 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 Y1 - 2005 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Jin, Wen A1 - Ehrentreich-Förster, Eva A1 - Ge, Bixia A1 - Lisdat, Fred A1 - Büttemeyer, R. A1 - Wollenberger, Ursula T1 - Cytochrome c based superoxide sensor for in vivo application Y1 - 1999 ER -