Highly Activated Terminal Carbon Monoxide Ligand in an Iron-Sulfur Cluster Model of FeMco with Intermediate Local Spin State at Fe.

ABSTRACT: Nitrogenases, the enzymes that convert N₂ to NH₃, also catalyze the reductive coupling of CO to yield hydrocarbons. CO-coordinated species of nitrogenase clusters have been isolated and used to infer mechanistic information. However, synthetic FeS clusters displaying CO ligands remain rare, which limits benchmarking. Starting from a synthetic cluster that models a cubane portion of the FeMo cofactor (FeMoco), including a bridging carbyne ligand, we report a heterometallic tungsten-iron-sulfur cluster with a single terminal CO coordination in two oxidation states with a high level of CO activation (ν_CO = 1851 and 1751 cm^-1). The local Fe coordination environment (2S, 1C, 1CO) is identical to that in the protein making this system a suitable benchm

SUBMITTER: Le LNV 

PROVIDER: S-EPMC10910499 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature