期刊
CHEMELECTROCHEM
卷 4, 期 4, 页码 913-919出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/celc.201600776
关键词
electrochemistry; enzyme catalysis; mesoporous materials; microperoxidase; spectroelectrochemistry
资金
- Unicat Cluster of Excellence (Deutsche Forschungsgemeinschaft) [EXC 314/2]
- Albert-Ludwigs-University Freiburg
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.
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