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化学学报
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化学学报 ›› 1976, Vol. 34 ›› Issue (1): 1-16.    下一篇

论文

固氮酶的活性中心模型和催化作用机理

厦门大学化学系催化教研室固氮研究组   

  1. 厦门大学化学系催化教研室固氮研究组
  • 投稿日期:1975-05-15 发布日期:2013-06-03

A MODEL OF NITROGENASE ACTIVE-CENTER AND MECHANISM OF NITROGENASE CATALYSIS

LABORATORY OF CATALYSIS, CHEMISTRY DEPARTMENT, AMOY UNIVERSITY   

  1. LABORATORY OF CATALYSIS, CHEMISTRY DEPARTMENT, AMOY UNIVERSITY
  • Received:1975-05-15 Published:2013-06-03

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本文根据固氮酶已知的反应和络合催化原理,讨论了固氮酶的作用机理和活性中心结构.提出了由类立方烷结构的Fe2S2·Mo2O2八原子簇构成的一对偶联的两钼一铁(2Mo-1Fe)三核活性中心模型,并用以阐明固氮酶各种底物的酶促还原反应机理,包括放氢反应机理,以及一氧化碳不抑制放氢反应而对其他底物的酶促还原反应显出竞争性与非竞争性的混合型抑制特征的原因,提出了二步ATP驱动的“电子活化”机理,并用以解释ATP/2e-的比值和不需还原剂的ATP酶促水解.指出了这二步ATP驱动的“电子活化”与绿色植物光合作用中的二步光驱动电子传递的紧密对应关系.

Based upon the known reactions of nitrogenase and the principles of coordination catalysis,a model of nitrogenase active-center is proposed.An octa-atomic cluster,Fe2S2·Mo2O2,of pseudo-onbane-type structure is supposed to form a coupled twin of trinuclear(2Mo-1Fe) active-centers,which also catalyze the reduction of H+ to H2.With this model,mechanisms of all the known nitrogenase-catalyzed reactions are explained,together with the non-inhibition of the hydrogen-evolution reaction by CO,and the mixed character of inhibition of other nitrogenase-catalyzed reactions.