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

Dhanashree Selvan | Zendy; Yelu Shi | Zendy; Pallavi Prasad | Zendy; Skyler Crane | Zendy; Yong Zhang | Zendy; Saumen Chakraborty | Zendy

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

Author(s) -

Dhanashree Selvan,

Yelu Shi,

Pallavi Prasad,

Skyler Crane,

Yong Zhang,

Saumen Chakraborty

Publication year - 2020

Publication title -

dalton transactions

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.98

H-Index - 184

eISSN - 1477-9234

pISSN - 1477-9226

DOI - 10.1039/c9dt04913d

Subject(s) - reactivity (psychology) , copper , hydrogenase , oxygen , chemistry , combinatorial chemistry , chemical engineering , enzyme , biochemistry , organic chemistry , engineering , medicine , alternative medicine , pathology

The O 2 reactivity of an artificial biomolecular hydrogenase, the nickel binding protein (NBP) is investigated. Kinetic analyses revealed a complete 4e - reduction of O 2 to H 2 O under catalytic conditions with associated k 0 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 O 2 activation by NBP.

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