Comprehensive reaction mechanisms at and near the Ni–Fe active sites of [NiFe] hydrogenases. Issue 13 (13th March 2018)

• Record Type: Journal Article
• Authors: Tai, Hulin; Higuchi, Yoshiki; Hirota, Shun
• Is Part Of: Dalton transactions. Volume 47:Issue 13(2018)
• Page Start: 4408
• Page End: 4423
• Publication Date: 2018-03-13
• Subjects: Chemistry, Inorganic -- Periodicals; Chemistry, Physical and theoretical -- Periodicals; Chemistry, Inorganic -- Periodicals; 546.05
• DOI: 10.1039/c7dt04910b
• Languages: English
• ISSNs: 1477-9226

Abstract

Abstract : We overview recent advances in the mechanisms at and near the Ni–Fe sites of [NiFe] hydrogenases for activation–inactivation, catalytic reaction, proton transfer, and O2 -tolerance. Abstract : [NiFe] hydrogenase (H2 ase) catalyzes the oxidation of dihydrogen to two protons and two electrons and/or its reverse reaction. For this simple reaction, the enzyme has developed a sophisticated but intricate mechanism with heterolytic cleavage of dihydrogen (or a combination of a hydride and a proton), where its Ni–Fe active site exhibits various redox states. Recently, thermodynamic parameters of the acid–base equilibrium for activation–inactivation, a new intermediate in the catalytic reaction, and new crystal structures of [NiFe] H2 ases have been reported, providing significant insights into the activation–inactivation and catalytic reaction mechanisms of [NiFe] H2 ases. This Perspective provides an overview of the reaction mechanisms of [NiFe] H2 ases based on these new findings.