Nitrogenase assembly

被引:59
作者
Hu, Yilin [1 ]
Ribbe, Markus W. [1 ]
机构
[1] Univ Calif Irvine, Dept Mol Biol & Biochem, Irvine, CA 92687 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2013年 / 1827卷 / 8-9期
基金
美国国家卫生研究院;
关键词
Nitrogenase; Metallocluster; Assembly; P-cluster; M-cluster; IRON-MOLYBDENUM COFACTOR; BRIDGED DOUBLE CUBANES; PROTEIN ALPHA-SUBUNIT; MOFE-PROTEIN; P-CLUSTER; AZOTOBACTER-VINELANDII; FEMO COFACTOR; MOLECULAR INSIGHTS; CRYSTALLOGRAPHIC STRUCTURE; STRUCTURAL BASIS;
D O I
10.1016/j.bbabio.2012.12.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Nitrogenase contains two unique metalloclusters: the P-cluster and the M-cluster. The assembly processes of P- and M-clusters are arguably the most complicated processes in bioinorganic chemistry. There is considerable interest in decoding the biosynthetic mechanisms of the P- and M-clusters, because these clusters are not only biologically important, but also chemically unprecedented. Understanding the assembly mechanisms of these unique metalloclusters is crucial for understanding the structure-function relationship of nitrogenase. Here, we review the recent advances in this research area, with an emphasis on our work that provide important insights into the biosynthetic pathways of these high-nuclearity metal centers. This article is part of a Special Issue entitled: Metals in Bioenergetics and Biomimetics Systems. (C) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:1112 / 1122
页数:11
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