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

Neumann B, Kielb P, Rustam L, Fischer A, Weidinger IM, Wollenberger U (2017)


Publication Type: Journal article

Publication year: 2017

Journal

Book Volume: 4

Pages Range: 913-919

Journal Issue: 4

DOI: 10.1002/celc.201600776

Abstract

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 +500 mV 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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How to cite

APA:

Neumann, B., Kielb, P., Rustam, L., Fischer, A., Weidinger, I.M., & Wollenberger, U. (2017). Bioelectrocatalytic Reduction of Hydrogen Peroxide by Microperoxidase-11 Immobilized on Mesoporous Antimony-Doped Tin Oxide. ChemElectroChem, 4(4), 913-919. https://doi.org/10.1002/celc.201600776

MLA:

Neumann, Bettina, et al. "Bioelectrocatalytic Reduction of Hydrogen Peroxide by Microperoxidase-11 Immobilized on Mesoporous Antimony-Doped Tin Oxide." ChemElectroChem 4.4 (2017): 913-919.

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