Organometallic and Cluster Chemistry in M+I40etalloenzymes with Reducing Activities

通过配位/有机金属化学、结构生物学和理论化学的结合，我们承担了还原酶的化学研究，其重要性最近被注意到与社会对能量和食物的需求有关。我们在这个项目中取得的成就超出了我们的预期，我们已经取得了重要的成果，为理解还原酶在簇活性部位的酶功能提供了线索。我们成功地合成了固氮酶和氢酶活性中心的有利模型，并阐明了它们的物理化学性质，使我们能够研究这些酶的化学。通过对新合成的激活氮素的双核配合物的理论分析，揭示了它的反应机理，也为固氮酶和氢酶的反应机理提供了重要的信息。我们还在耐氧[NiFe]氢酶的结构中发现了新的[4Fe-3S]簇。

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.