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首页> 外文期刊>Dalton transactions: An international journal of inorganic chemistry >Breaking the N-2 triple bond: insights into the nitrogenase mechanism
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Breaking the N-2 triple bond: insights into the nitrogenase mechanism

机译：打破N-2三键：深入了解固氮酶的机理

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摘要

Nitrogenase is the metalloenzyme that performs biological nitrogen fixation by catalyzing the reduction of N-2 to ammonia. Understanding how the nitrogenase active site metal cofactor (FeMo-cofactor) catalyzes the cleavage of the N-2 triple bond has been the focus of intense study for more than 50 years. Goals have included the determination of where and how substrates interact with the FeMo-cofactor, and the nature of reaction intermediates along the reduction pathway. Progress has included the trapping of intermediates formed during turnover of non-physiological substrates ( e. g., alkynes, CS2) providing insights into how these molecules interact with the nitrogenase FeMo-cofactor active site. More recently, substrate-derived species have been trapped at high concentrations during the reduction of N-2, a diazene, and hydrazine, providing the first insights into binding modes and possible mechanisms for N-2 reduction. A comparison of the current state of knowledge of the trapped species arising from non-physiological substrates and nitrogenous substrates is beginning to reveal some of the intricacies of how nitrogenase breaks the N-2 triple bond.
机译：固氮酶是通过催化N-2还原为氨而进行生物固氮的金属酶。 50多年来，了解固氮酶活性位点金属辅因子（FeMo-cofactor）如何催化N-2三键的裂解一直是研究的重点。目标包括确定底物在何处以及如何与FeMo-辅因子相互作用，以及沿着还原途径的反应中间体的性质。进展包括捕获在非生理底物（例如炔烃，CS2）周转期间形成的中间体，从而提供了对这些分子如何与固氮酶FeMo-辅因子活性位点相互作用的见解。最近，在还原N-2，重氮和肼的过程中，高浓度捕获了底物来源的物质，从​​而为结合模式和N-2还原的可能机理提供了第一见解。对由非生理性底物和含氮底物引起的被捕物质的当前知识状态的比较开始揭示出氮酶如何破坏N-2三键的某些复杂性。

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