Nitrogenase-Relevant Reactivity of a Synthetic Iron-Sulfur-Carbon Site.

ABSTRACT: Simple synthetic compounds with only S and C donors offer a ligation environment similar to the active site of nitrogenase (FeMoco) and thus demonstrate reasonable mechanisms and geometries for N₂ binding and reduction in nature. We recently reported the first example of N₂ binding at a mononuclear iron site supported by only S and C donors. In this work, we report experiments that examine the mechanism of N₂ binding in this system. The reduction of an iron(II) tris(thiolate) complex with 1 equiv of KC₈ leads to a thermally unstable intermediate, and a combination of Mössbauer, EPR, and X-ray absorption spectroscopies identifies it as a high-spin (S = 3/2) iron(I) species that maintains coordination of all three sulfur atoms. DFT calculati

SUBMITTER: Speelman AL 

PROVIDER: S-EPMC7251483 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature