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

被引:88
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
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.
引用
收藏
页码:179 / 193
页数:15
相关论文
共 94 条
  • [91] Yang XD, 1997, J BIOL CHEM, V272, P9683
  • [92] YU L, 1987, J BIOL CHEM, V262, P1137
  • [93] ASSIGNMENT OF THE HISTIDINE AXIAL LIGANDS TO THE CYTOCHROME-BH AND CYTOCHROME-BL COMPONENTS OF THE BC1 COMPLEX FROM RHODOBACTER-SPHAEROIDES BY SITE-DIRECTED MUTAGENESIS
    YUN, CH
    CROFTS, AR
    GENNIS, RB
    [J]. BIOCHEMISTRY, 1991, 30 (27) : 6747 - 6754
  • [94] Electron transfer by domain movement in cytochrome bc1
    Zhang, ZL
    Huang, LS
    Shulmeister, VM
    Chi, YI
    Kim, KK
    Hung, LW
    Crofts, AR
    Berry, EA
    Kim, SH
    [J]. NATURE, 1998, 392 (6677) : 677 - 684