CAJ | 학술논문

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，然而，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．
고담매시모사미생물재상온상압하고담성안적주요최화제，기최화궤리화화학모의시국제상장기치력연구적대상．진관인문이경게시료고담매최화활성중심－철목보기(FeMo-co)MoFe7S9(R-고저몽산)적결구，연이，유관FeMo-co생물합성적상세도경화기중포함적목철전이화이용；고담매재나사활성위화안십요모식결합N2，C2H2、CO등다충저물혹억제제；이급기중섭급적전자화질자전체과정등허다문제，지금상유대해결．본문장종술저사문제적연구진전화하문대학고담조최근오년래적상관연구공작．
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 MoFe7S9 (Rhomocitrate), 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.