Synthesis, Properties, and Electrochemical Proton Reduction of a Homoleptic Tetrathiolato Ni-Site Model of [NiFe]-Hydrogenase.

ABSTRACT: [NiFe]-hydrogenase enzymes process H₂ at a nonplanar tetracysteinato-Ni site, the sole participator in proton binding/redox chemistry during turnover. With the objective of assessing whether a simple tetrahedral/tetrathiolato-Ni²⁺ core could promote H₂ evolution reaction (HER), we synthesized (Et₄N)₂[Ni(S-p-CF₃-Ph)₄] (1) employing para-trifluoromethylbenzenethiolate (^-S-p-CF₃-Ph) as a Ni-site analog of [NiFe]-hydrogenase. Spectroscopic measurements and X-ray crystallography confirm the distorted tetrahedral geometry of 1. Dissolution of 1 results in partial thiolate dissociation and formation of S,S-bridged complexes such as (Et₄

SUBMITTER: Yosen BA 

PROVIDER: S-EPMC12628296 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature