Biosynthesis of the Iron-Molybdenum Cofactor of Nitrogenase

被引：264

作者：

Rubio, Luis M. ^{[1
]}

Ludden, Paul W. ^{[2
]}

机构：

[1] Univ Calif Berkeley, Dept Plant & Microbial Biol, Berkeley, CA 94720 USA

[2] So Methodist Univ, Off Provost, Dallas, TX 75275 USA

来源：

ANNUAL REVIEW OF MICROBIOLOGY | 2008年 / 62卷

基金：

美国国家卫生研究院;

关键词：

nitrogen fixation; nif; FeMo-co; iron-sulfur; NifDK; MoFe protein;

D O I：

10.1146/annurev.micro.62.081307.162737

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The iron-molybdenum cofactor (FeMo-co), located at the active site of the molybdenum nitrogenase, is one of the most complex metal cofactors known to date. During the past several years, an intensive effort has been made to purify the proteins involved in FeMo-co synthesis and incorporation into nitrogenase. This effort is starting to provide insights into the structures of the FeMo-co biosythetic intermediates and into the biochemical details of FeMo-co synthesis.

引用

页码：93 / 111

页数：19

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