Reactivation of standard [NiFe]-hydrogenase and bioelectrochemical catalysis of proton reduction and hydrogen oxidation in a mediated-electron-transfer system

Bioelectrochemistry
Saeko ShiraiwaKenji Kano

Abstract

Standard [NiFe]-hydrogenase from Desulfovibrio vulgaris Miyazaki F (DvMF-H2ase) catalyzes the uptake and production of hydrogen (H2) and is a promising biocatalyst for future energy devices. However, DvMF-H2ase experiences oxidative inactivation under oxidative stress to generate Ni-A and Ni-B states. It takes a long time to reactivate the Ni-A state by chemical reduction, whereas the Ni-B state is quickly reactivated under reducing conditions. Oxidative inhibition limits the application of DvMF-H2ase in practical devices. In this research, we constructed a mediated-electron-transfer system by co-immobilizing DvMF-H2ase and a viologen redox polymer (VP) on electrodes. The system can avoid oxidative inactivation into the Ni-B state at high electrode potentials and rapidly reactivate the Ni-A state by electrochemical reduction of VP. H2 oxidation and H+ reduction were realized by adjusting the pH from a thermodynamic viewpoint. Using carbon felt as a working-electrode material, high current densities-up to (200 ± 70) and -(100 ± 9) mA cm-3 for the H2-oxidation and H+-reduction reactions, respectively-were attained.

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Citations

Aug 14, 2019·Biotechnology and Bioengineering·Lu Yuan, Jamin Koo
Feb 20, 2020·Chemistry : a European Journal·John Charles RuthAlfred M Spormann
Apr 13, 2021·Nature Catalysis·Steffen HardtNicolas Plumeré
Dec 17, 2021·Bioconjugate Chemistry·Rafael T P da SilvaSusana I Córdoba de Torresi

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