Open AccessThe oxygen reactivity of an artificial hydrogenase designed in a reengineered copper storage protein
Author(s) -
Dhanashree Selvan,
Yong 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.