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

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.