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

Dhanashree Selvan, Yelu Shi, Pallavi Prasad, Skyler Crane, Yong Zhang, Saumen Chakraborty

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)1928-1934
Number of pages7
JournalDalton Transactions
Volume49
Issue number6
DOIs
StatePublished - 14 Feb 2020

Fingerprint

Dive into the research topics of 'The oxygen reactivity of an artificial hydrogenase designed in a reengineered copper storage protein'. Together they form a unique fingerprint.

Cite this