55148
2017
2017
eng
913
919
7
4
4
article
Wiley-VCH
Weinheim
1
2017-04-13
2017-01-11
--
Bioelectrocatalytic Reduction of Hydrogen Peroxide by Microperoxidase-11 Immobilized on Mesoporous Antimony-Doped Tin Oxide
The heme-undecapeptide microperoxidase-11 (MP-11) was immobilized on mesoporous antimony-doped tin oxide (ATO) thin-film electrodes modified with the positively charged binding promotor polydiallyldimethylammonium chloride. Surface concentrations of MP-11 of 1.5 nmol cm(-2) were sufficiently high to enable spectroelectrochemical analyses. UV/Vis spectroscopy and resonance Raman spectroscopy revealed that immobilized MP-11 adopts a six-coordinated low-spin conformation, as in solution in the presence of a polycation. Cathodic reduction of hydrogen peroxide at potentials close to +500mV versus Ag/AgCl indicates that the reaction proceeds via a Compound I-type like intermediate, analogous to natural peroxidases, and confirms mesoporous ATO as a suitable host material for adsorbing the heme-peptide in its native state. A hydrogen peroxide sensor is proposed by using the bioelectrocatalytic properties of the MP-11-modified ATO.
ChemElectrChem
10.1002/celc.201600776
2196-0216
wos:2017
WOS:000399641500017
Wollenberger, U (reprint author), Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25, D-14476 Potsdam, Germany., uwollen@uni-potsdam.de
Unicat Cluster of Excellence (Deutsche Forschungsgemeinschaft) [EXC 314/2]; Albert-Ludwigs-University Freiburg
2022-06-13T06:02:09+00:00
sword
importub
filename=package.tar
43963078efd6933f12c5008ccda6eb38
Wollenberger, Ulla
false
true
Bettina Neumann
Patrycja Kielb
Lina Rustam
Anna Fischer
Inez M. Weidinger
Ulla Wollenberger
eng
uncontrolled
electrochemistry
eng
uncontrolled
enzyme catalysis
eng
uncontrolled
mesoporous materials
eng
uncontrolled
microperoxidase
eng
uncontrolled
spectroelectrochemistry
Biowissenschaften; Biologie
Institut für Biochemie und Biologie
Referiert
Import
51485
2018
2018
eng
13810
13814
5
42
57
article
Wiley-VCH
Weinheim
1
2018-08-23
2018-08-23
--
Enzyme-Polymer Conjugates as Robust Pickering Interfacial Biocatalysts for Efficient Biotransformations and One-Pot Cascade Reactions
Despite the rapid development of Pickering interfacial catalysis (PIC) at liquid-liquid interfaces with chemocatalysts, the use of unstable biocatalysts at emulsion interfaces remains a technical challenge. Herein, we present a Pickering interfacial biocatalysis (PIB) platform based on robust and recyclable enzyme-polymer conjugates that act as both catalytic sites and stabilizers at the interface of Pickering emulsions. The conjugates were prepared by growing poly(N-isopropylacrylamide) on a fragile enzyme, benzaldehyde lyase, under physiological conditions. The mild in situ conjugation process preserved the enzyme structure, and the conjugates were used to emulsify a water-organic two-phase system into a stable Pickering emulsion, leading to a significantly larger interfacial area and a 270-fold improvement in catalytic performance as compared to the unemulsified two-phase system. The PIB system could be reused multiple times. Conjugates of other enzymes were also fabricated and applied for cascade reactions.
Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition
10.1002/anie.201806049
30141281
1433-7851
1521-3773
wos:2018
WOS:000446826200014
Wu, CZ (reprint author), Univ Southern Denmark, DIAS, Campusvej 55, DK-5230 Odense, Denmark.; Wu, CZ (reprint author), Univ Southern Denmark, Dept Phys Chem & Pharm, Campusvej 55, DK-5230 Odense, Denmark., wu@sdu.dk
Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [WU 814/1-1]; China Scholarship Council (CSC)China Scholarship Council
2021-08-06T04:55:21+00:00
sword
importub
filename=package.tar
f746e956e57be6188c208b6e7db64f8b
Wu, Changzhu
false
true
Zhiyong Sun
Ulrich Glebe
Himanshu Charan
Alexander Böker
Changzhu Wu
eng
uncontrolled
biphasic catalysis
eng
uncontrolled
cascade reactions
eng
uncontrolled
enzyme catalysis
eng
uncontrolled
enzyme-polymer conjugates
eng
uncontrolled
Pickering interfacial catalysis
Chemie und zugeordnete Wissenschaften
Institut für Chemie
Referiert
Import
46186
2017
2017
eng
15583
15587
5
23
article
Wiley-VCH
Weinheim
1
--
--
--
The 1,6,7,12-Tetraazaperylene Bridging Ligand as an Electron Reservoir and Its Disulfonato Derivative as Redox Mediator in an Enzyme-Electrode Process
The homodinuclear ruthenium(II) complex [{Ru(l-N4Me2)}(2)(-tape)](PF6)(4) {[1](PF6)(4)} (l-N4Me2=N,N-dimethyl-2,11-diaza[3.3](2,6)-pyridinophane, tape=1,6,7,12-tetraazaperylene) can store one or two electrons in the energetically low-lying * orbital of the bridging ligand tape. The corresponding singly and doubly reduced complexes [{Ru(l-N4Me2)}(2)(-tape(.-))](PF6)(3) {[2](PF6)(3)} and [{Ru(l-N4Me2)}(2)(-tape(2-))](PF6)(2) {[3](PF6)(2)}, respectively, were electrochemically generated, successfully isolated and fully characterized by single-crystal X-ray crystallography, spectroscopic methods and magnetic susceptibility measurements. The singly reduced complex [2](PF6)(3) contains the -radical tape(.-) and the doubly reduced [3](PF6)(2) the diamagnetic dianion tape(2-) as bridging ligand, respectively. Nucleophilic aromatic substitution at the bridging tape in [1](4+) by two sulfite units gave the complex [{Ru(l-N4Me2)}(2){-tape-(SO3)(2)}](2+) ([4](2+)). Complex dication [4](2+) was exploited as a redox mediator between an anaerobic homogenous reaction solution of an enzyme system (sulfite/sulfite oxidase) and the electrode via participation of the low-energy *-orbital of the disulfonato-substituted bridging ligand tape-(SO3)(2)(2-) (E-red1=-0.1V versus Ag/AgCl/1m KCl in water).
Chemistry - a European journal
10.1002/chem.201703639
28869692
0947-6539
1521-3765
wos:2017
WOS:000414633200004
Holdt, HJ (reprint author), Univ Potsdam, Inst Chem, Karl Liebknecht Str 24-25, D-14476 Potsdam, Germany.; Kruger, HJ (reprint author), Tech Univ Kaiserslautern, Fachbereich Chem, Anorgan Chem, Erwin Schrodinger Str Geb 54, D-67663 Kaiserslautern, Germany., krueger@chemie.uni-kl.de; holdt@uni-potsdam.de
University of Potsdam; Deutsche Forschungsgemeinschaft (DFG) [SFB-TRR-88]; University of Kaiserslautern
importub
2020-04-19T23:22:01+00:00
filename=package.tar
0184ffd223ab803fae5c01446ee4c097
Thomas Martin Brietzke
Thomas Dietz
Alexandra Kelling
Uwe Schilde
Juliana Bois
Harald Kelm
Manuel Reh
Markus Schmitz
Thomas Koerzdoerfer
Silke Leimkühler
Ulla Wollenberger
Hans-Joerg Krueger
Hans-Jürgen Holdt
eng
uncontrolled
electrochemistry
eng
uncontrolled
enzyme catalysis
eng
uncontrolled
N-ligands
eng
uncontrolled
redox-active ligands
eng
uncontrolled
ruthenium
Institut für Biochemie und Biologie
Referiert
Import
44971
2016
2016
eng
2853
2857
5
8
article
Wiley-VCH
Weinheim
HESS Collaboration
1
--
--
--
Enzymatic Cleavage of Aryl Acetates
Seven enzymes have been screened for the cleavage of aryl acetates. Phenyl and naphthyl acetates react with lipases and esterases, whereas the sterically demanding anthracene acetate gave a conversion only with porcine liver esterase and esterase 2 from Bacillus subtilis (BS2). These two enzymes have been employed on a preparative (0.5 mmol) scale and afforded cleavage products in 91 and 94% yields, even for anthracene acetate. Thus, this method is superior to chemical cleavage with catalytic amounts of sodium methoxide (Zemplen conditions), which gave only low conversions. Finally, regioselectivity has been achieved with an anthracene bisacetate, in which an ethyl group controls the cleavage of the first acetate. This indicates that steric interactions play a crucial role in the enzymatic cleavage of aryl acetates, which might be interesting for future applications or the development of enzyme inhibitors.
ChemCatChem : heterogeneous & homogeneous & bio- & nano-catalysis ; a journal of ChemPubSoc Europe
10.1002/cctc.201600678
1867-3880
1867-3899
wos2016:2019
WOS:000386917800017
Linker, T (reprint author), Univ Potsdam, Dept Chem, Karl Liebknecht Str 24-25, D-14476 Potsdam, Germany., linker@uni-potsdam.de
University of Potsdam; University of Greifswald
importub
2020-03-22T14:36:01+00:00
filename=package.tar
cd74aca1cad908f0a03c35d6b56a0ea9
Marcel Bauch
Dominique Böttcher
Uwe T. Bornscheuer
Torsten Linker
eng
uncontrolled
arenes
eng
uncontrolled
enzyme catalysis
eng
uncontrolled
regioselectivity
eng
uncontrolled
steric hindrance
eng
uncontrolled
substituent effects
Institut für Chemie
Referiert
Import
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
38694
2015
2015
eng
2313
2317
5
15
7
article
Wiley-VCH
Weinheim
1
--
--
--
Galactose Oxidase Variants for the Oxidation of Amino Alcohols in Enzyme Cascade Synthesis
The use of selected engineered galactose oxidase (GOase) variants for the oxidation of amino alcohols to aldehydes under mild conditions in aqueous systems is reported. GOase variant F-2 catalyses the regioselective oxidation of N-carbobenzyloxy (Cbz)-protected 3-amino-1,2-propanediol to the corresponding -hydroxyaldehyde which was then used in an aldolase reaction. Another variant, M3-5, was found to exhibit activity towards free and N-Cbz-protected aliphatic and aromatic amino alcohols allowing the synthesis of lactams such as 3,4-dihydronaphthalen-1(2H)-one, 2-pyrrolidone and valerolactam in one-pot tandem reactions with xanthine dehydrogenase (XDH) or aldehyde oxidase (PaoABC).
ChemCatChem : heterogeneous & homogeneous & bio- & nano-catalysis ; a journal of ChemPubSoc Europe
10.1002/cctc.201500218
1867-3880
1867-3899
wos:2015
WOS:000359066500005
Carnell, AJ (reprint author), Univ Liverpool, Robert Robinson Labs, Dept Chem, Crown St, Liverpool L69 7ZD, Merseyside, England., a.j.carnell@liverpool.ac.uk; nicholas.turner@manchester.ac.uk
Innovative Medicines Initiative Joint Undertaking [115360]; European
Union; EFPIA; Science and Industry Endowment (SIEF); Engineering and
Physical Sciences Research Council (EPSRC); Royal Society Wolfson Merit
Award
Susanne Herter
Shane M. McKenna
Andrew R. Frazer
Silke Leimkühler
Andrew J. Carnell
Nicholas J. Turner
eng
uncontrolled
aldehyde oxidase
eng
uncontrolled
amino alcohols
eng
uncontrolled
cascade reactions
eng
uncontrolled
enzyme catalysis
eng
uncontrolled
lactams
Institut für Biochemie und Biologie
Referiert
34580
2013
2013
eng
2544
2555
12
9
article
Beilstein-Institut zur Förderung der Chemischen Wissenschaften
Frankfurt, Main
1
--
--
--
Bidirectional cross metathesis and ring-closing metathesis/ring opening of a C-2-symmetric building block: a strategy for the synthesis of decanolide natural products
Starting from the conveniently available ex-chiral pool building block (R,R)-hexa-1,5-diene-3,4-diol, the ten-membered ring lactones stagonolide E and curvulide A were synthesized using a bidirectional olefin-metathesis functionalization of the terminal double bonds. Key steps are (i) a site-selective cross metathesis, (ii) a highly diastereoselective extended tethered RCM to furnish a (Z,E)-configured dienyl carboxylic acid and (iii) a Ru-lipase-catalyzed dynamic kinetic resolution to establish the desired configuration at C9. Ring closure was accomplished by macrolactonization. Curvulide A was synthesized from stagonolide E through Sharpless epoxidation.
Beilstein journal of organic chemistry
10.3762/bjoc.9.289
1860-5397
wos:2011-2013
WOS:000327709300002
Schmidt, B (reprint author), Univ Potsdam, Inst Chem, Karl Liebknecht Str 24-25, D-14476 Potsdam, Germany., bernd.schmidt@uni-potsdam.de
Deutsche Forschungsgemeinschaft (DFG) [Schm 1095/6-2]
Bernd Schmidt
Oliver Kunz
eng
uncontrolled
dienes
eng
uncontrolled
enzyme catalysis
eng
uncontrolled
lactones
eng
uncontrolled
metathesis
eng
uncontrolled
natural products
eng
uncontrolled
ruthenium
Institut für Chemie
Referiert
Open Access