Synthesis and Properties of Metal-Sulfur Clusters Consisting of Multiple Components

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Biological transformations of N2 and CO are mediated by the metallo-enzymes called nitrogenase and CO-dehydrogenase, respectively. Their active sites consist of sulfur, iron, and another transition metal, and their complex structures have been challenging synthetic targets. In this research project, we developed new synthetic reactions for Fe/S/O and V/Fe/S clusters in non-polar organic solvents. One of the important outcomes of this project is the synthesis of the [Fe8S6O] cluster which mimics the active site of nitrogenase. The bonding mode of its central oxygen atom gave us a clue to understand how the enzymatic active site works. Also to be noted is the synthesis of [VFe3S4-Fe] cluster which is structurally relevant to the active site of CO-dehydrogenase.