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

doi:10.1039/c9dt04913d

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

Department of Chemistry and Chemical Biology

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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 language	English
Pages (from-to)	1928-1934
Number of pages	7
Journal	Dalton Transactions
Volume	49
Issue number	6
DOIs	https://doi.org/10.1039/c9dt04913d
State	Published - 14 Feb 2020

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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.",

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AU - Selvan, Dhanashree

AU - Shi, Yelu

AU - Prasad, Pallavi

AU - Crane, Skyler

AU - Zhang, Yong

AU - Chakraborty, Saumen

PY - 2020/2/14

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N2 - 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.

AB - 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.

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VL - 49

SP - 1928

EP - 1934

JO - Dalton Transactions

JF - Dalton Transactions

IS - 6

ER -

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

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