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The oxygen reactivity of an artificial hydrogenase designed in a reengineered copper storage protein

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Abstract

The O2 reactivity of an artificial biomolecular hydrogenase, the nickel binding protein (NBP) is investigated. Kinetic analyses revealed a complete 4e reduction of O2 to H2O under catalytic conditions with associated k0 for ET in the order of 10−6 cm s−1. Protein destabilization and S oxygenation are contributing factors to the deactivation of NBP under oxic conditions. Computational studies provided insight into the S oxygenation and the reaction intermediates of a proposed mechanistic pathway for O2 activation by NBP.

Graphical abstract: The oxygen reactivity of an artificial hydrogenase designed in a reengineered copper storage protein

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Article information


Submitted
30 Dec 2019
Accepted
08 Jan 2020
First published
09 Jan 2020

Dalton Trans., 2020, Advance Article
Article type
Paper

The oxygen reactivity of an artificial hydrogenase designed in a reengineered copper storage protein

D. Selvan, Y. Shi, P. Prasad, S. Crane, Y. Zhang and S. Chakraborty, Dalton Trans., 2020, Advance Article , DOI: 10.1039/C9DT04913D

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