Studies on Biosynthesis and Catalysis of Metal-Sulfur Clusters

Abstract

Transition metal-sulfur clusters are ubiquitous as enzymatic cofactors and play critical roles in various molecular transformations. Their synthetic counterparts have been studied with a significant focus on structural and spectroscopic modeling in the past 50 years. However, applications of this class of compounds for other purposes remain limited. In this context, we have been working on applying synthetic metal-sulfur clusters to biochemical analysis and catalysis with great interest in the enzymatic N2-reducing cluster (FeMoco). Synthetic clusters function as artificial cofactors of enzymes. The resultant reconstituted proteins can perform catalytic reduction using a natural electron transfer system or help analyze an unidentified intermediate involved in the biosynthesis of FeMoco. In addition, we developed catalytic reduction reactions of inert small molecules (e.g. CO, CO₂, and N₂) promoted by synthetic clusters. This account overviews the series of research to deliver a brief perspective of the functional aspect of the synthetic metal-sulfur clusters.