Organometallic and Cluster Chemistry in M+I40etalloenzymes with Reducing Activities

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Through the integration of coordination/organometallic chemistry, structural biology, and theoretical chemistry, we have undertaken the chemical study of reductases, the importance of which has been noticed recently in connection with social needs for energy and food. Our accomplishments in this program have exceeded our expectations, and we have achieved significant results that provide clues in understanding the enzymatic function of reductases at the cluster active sites. We have succeeded in synthesizing favourable models of the active-sites of nitrogenase and hydrogenase, and their physicochemical properties have been clarified, enabling us to study the chemistry of these enzymes. From the theoretical analysis of the newly synthesized dinuclear complex that activates dinitrogen, we revealed its reaction mechanism, which also provides us with important information concerning the reaction mechanisms of nitrogenase and hydrogenases. We have also discovered the novel[4Fe-3S] cluster in the structure of an oxygen-tolerant[NiFe] hydrogenase.