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化学进展 1997, Vol. 9 Issue (03): 265- 前一篇   后一篇

• 综述与评论 •

固氮酶活性中心FeMo-Cofactor对N2活化方式的探讨*

张纯喜;樊红军;刘秋田   

  1. (中国科学院福建物质结构研究所结构化学国家重点实验室 福州 350002)
  • 收稿日期:1996-08-01 修回日期:1996-12-01 出版日期:1997-09-24 发布日期:1997-09-24

Discussion on the Activation Models of Dinitrogen by FeMo-Cofactor in Nitrogenase

Zhang Chunxi;Fan Hongjun;Liu Qiutian   

  1. (State Key Laboratory of Structural Chemistry, Fu jian Institute of Research on the Structure of Matter, Chinese Acadamy of Sciences, Fuzhou 350002, China)
  • Received:1996-08-01 Revised:1996-12-01 Online:1997-09-24 Published:1997-09-24

结合实验和理论计算的结果, 讨论了固氮酶的活性中心铁钼辅基(FeMo-co-facto r) 对N2 的各种活化方式, 并在此基础上提出了一种新模型, 即N2 在FeMo2cofacto r 的内部以“4Fe 端基配位+2Fe 侧基配位”的方式被活化,N2 的三重键完全断裂, 断裂产生的两个含N 的碎片分别偏向两侧的“窗口”, 再在H 的进攻下被还原为NH3, 并分别从两侧的“窗口”离去。

On discussing some activation models of dinitrogen by the active center,FeMo-cofactor of the nitrogenase based on experiments and theoretical calculations, a new activation model of dinitrogen has been suggested. In this model, the dinitrogen is coordinated to 4Fe and 2Fe atoms of FeMo-cofactor in“end-on”and“side-on”modes respectively, and is activated inside the FeMo-cofactor. Accompanying the complete cleavage of N≡N triple bond, both fragments containing Natomshift to the respective“window”on both sides of the FeMo-cofactor and are reduced in the hydrogenation process to form NH3which get off from the nearby“windows”.

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[2] 张纯喜. 固氮酶的固氮机理和其人工模拟问题的探讨[J]. 化学进展, 1997, 9(02): 131-.