Chloride- and Hydrosulfide-Bound 2Fe Complexes as Models of the Oxygen-Stable State of [FeFe] Hydrogenase.

[FeFe] hydrogenases demonstrate remarkable catalytic efficiency in hydrogen evolution and oxidation processes. However, susceptibility of these enzymes to oxygen-induced degradation impedes their practical deployment in hydrogen-production devices and fuel cells. Recent investigations into the oxygen-stable (H) state of the H-cluster revealed its inherent capacity to resist oxygen degradation. Herein, we present findings on Cl- and SH-bound [2Fe-2S] complexes, bearing relevance to the oxygen-stable state within a biological context. A characteristic attribute of these complexes is the terminal Cl/SH ligation to the iron center bearing the CO bridge. Structural analysis of the t-Cl demonstrates a striking resemblance to the H state of DdHydAB and CbA5H. The t-Cl/t-SH exhibit reversible oxidation, with both redox species, electronically, being the first biomimetic analogs to the H and H states. These complexes exhibit notable resistance against oxygen-induced decomposition, supporting the potential oxygen-resistant nature of the H and H states. The swift reductive release of the Cl-/SH-group demonstrates its labile and kinetically controlled binding. The findings garnered from these investigations offer valuable insights into properties of the enzymatic O-stable state, and key factors governing deactivation and reactivation conversion. This work contributes to the advancement of bio-inspired molecular catalysts and the integration of enzymes and artificial catalysts into H-evolution devices and fuel-cell applications.