| Literature DB >> 31971173 |
Dhanashree Selvan1, Yelu Shi2, Pallavi Prasad1, Skyler Crane1, Yong Zhang2, Saumen Chakraborty1.
Abstract
The O2 reactivity of an artificial biomolecular hydrogenase, the class="Gene">nickel binding protein (<class="Chemical">span class="Gene">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.Entities:
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Year: 2020 PMID: 31971173 PMCID: PMC7193703 DOI: 10.1039/c9dt04913d
Source DB: PubMed Journal: Dalton Trans ISSN: 1477-9226 Impact factor: 4.390