固氮酶催化作用机理及其化学模拟

固氮酶是某些微生物在常温常压下固氮成氨的主要催化剂，其催化机理和化学模拟是国际上长期致力研究的对象。尽管人们已经揭示了固氮酶催化活性中心——铁钼辅基（FeMo-co)MoFe7S9（R-高柠檬酸）的结构，然铡，有关FeMo-co生物合成的详细途径和其中包含的钼铁转移和利用；固氮酶在哪些活性位和按什么模式结合N2，C2H2、CO等多种底物或抑制剂；以及其中涉及的电子和质子传递过程等许多问题，至今尚有待解决。本文将综述这些问题的研究进展和厦门大学固氮组最近五年来的相关研究工作。

Catalytic Mechanism of Nitrogen Reduction by Nitrogenase and its Chemical Modeling

Nitrogenase catalyzes the reduction of dinitrogen to ammonia coupled to the hydrolysis of ATP, which is central to the process of biological nitrogen fixation. X ray crystallographic structures has revealed its catalytic metal center FeMo cofactor as a cage structure of MoFe 7S 9( R homocitrate), in which the homocitrate coordinate bidentately to molybdenum. Recent efforts towards establishing the mechanism of activation of nitrogen around the metal center and the early biosynthesis process of FeMo co are reviewed, which reflect a combination of structural, spectroscopic, synthetic, biochemical and theoretical approaches to this challenging problem pursued especially from the nitrogen fixation group of Xiamen University.