Bioelectrocatalytic Reduction of Hydrogen Peroxide by Microperoxidase-11 Immobilized on Mesoporous Antimony-Doped Tin Oxide

被引:14
|
作者
Neumann, Bettina [1 ]
Kielb, Patrycja [2 ]
Rustam, Lina [3 ]
Fischer, Anna [3 ]
Weidinger, Inez M. [2 ,4 ]
Wollenberger, Ulla [1 ]
机构
[1] Univ Potsdam, Inst Biochem & Biol, Karl Liebknecht Str 24-25, D-14476 Potsdam, Germany
[2] Tech Univ Berlin, Inst Chem, Str 17 Juni 135, D-10623 Berlin, Germany
[3] Univ Freiburg, Inst Inorgan & Analyt Chem, Albertstr 21, D-79104 Freiburg, Germany
[4] Tech Univ Dresden, Dept Chem & Food Chem, Helmholtzstr 10, D-01069 Dresden, Germany
来源
CHEMELECTROCHEM | 2017年 / 4卷 / 04期
关键词
electrochemistry; enzyme catalysis; mesoporous materials; microperoxidase; spectroelectrochemistry; DIRECT ELECTRON-TRANSFER; MONOLAYER-FUNCTIONALIZED ELECTRODES; ELECTROCATALYTIC REDUCTION; DIRECT ELECTROCHEMISTRY; GOLD ELECTRODE; CYTOCHROME-C; HEME; CARBON; INACTIVATION; SOLVENTS;
D O I
10.1002/celc.201600776
中图分类号
O646 [电化学、电解、磁化学];
学科分类号
081704 ;
摘要
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.
引用
收藏
页码:913 / 919
页数:7
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