Nitrogenase: standing at the crossroads

被引：215

作者：

Rees, DC

Howard, JB

机构：

[1] CALTECH, Howard Hughes Med Inst, Div Chem & Chem Engn, Pasadena, CA 91125 USA

[2] Univ Minnesota, Dept Biochem, Minneapolis, MN 55455 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2000年 / 4卷 / 05期

关键词：

D O I：

10.1016/S1367-5931(00)00132-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia, which is central to the process of biological nitrogen fixation. Recent progress towards establishing the mechanism of action of this complex metalloenzyme reflects the contributions of a combination of structural, biochemical, spectroscopic, synthetic and theoretical approaches to a challenging problem with implications for a range of biochemical and chemical systems.

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页码：559 / 566

页数：8

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