Synthetic Models for Nickel-Iron Hydrogenase Featuring Redox-Active Ligands.

ABSTRACT: The nickel-iron hydrogenase enzymes efficiently and reversibly interconvert protons, electrons, and dihydrogen. These redox proteins feature iron-sulfur clusters that relay electrons to and from their active sites. Reported here are synthetic models for nickel-iron hydrogenase featuring redox-active auxiliaries that mimic the iron-sulfur cofactors. The complexes prepared are Ni^II(μ-H)Fe^IIFe^II species of formula [(diphosphine)Ni(dithiolate)(μ-H)Fe(CO)₂(ferrocenylphosphine)]⁺ or Ni^IIFe^IFe^II complexes [(diphosphine)Ni(dithiolate)Fe(CO)₂(ferrocenylphosphine)]⁺ (diphosphine = Ph₂P(CH₂)₂PPh₂ or Cy₂P(CH₂)

SUBMITTER: Schilter D 

PROVIDER: S-EPMC5555595 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature