The coordination and function of the redox centres of the membrane-bound nitrate reductases

被引：90
作者：
Blasco, F
Guigliarelli, B
Magalon, A
Asso, M
Giordano, G
Rothery, RA
机构：
[1] CNRS, IBSM, Chim Bacterienne Lab, F-13402 Marseille 20, France
[2] CNRS, IBSM, Lab Bioenerget & Ingn Prot, F-13402 Marseille 20, France
[3] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada
来源：
CELLULAR AND MOLECULAR LIFE SCIENCES | 2001年 / 58卷 / 02期
关键词：
nitrate reductase; molybdenum cofactor; Fe-S] centres; haems;
D O I：
10.1007/PL00000846
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：
Under anaerobic conditions and in the presence of nitrate. the facultative anaerobe Escherichia coli synthesises an electron-transport chain comprising a primary dehydrogenase and the terminal membrane-bound nitrate reductase A (NarGHI). This review focuses on recent advances obtained on the structure and function of the three protein subunits of membrane-bound nitrate reductases. We discuss a global architecture for the Mo-bisMGD-containing subunit (NarG) and a coordination model for the four [Fe-S] centres of the electron-transfer subunit (NarH) and for the two b-type haems of the anchor subunit NarI.
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收藏
页码：179 / 193
页数：15
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