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