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

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.

引用

页码：179 / 193

页数：15

共 94 条

[1] Photosynthetic reaction centers
Allen, JP
Williams, JC
[J]. FEBS LETTERS, 1998, 438 (1-2) : 5 - 9
[2] CHARACTERIZATION OF MOLYBDENUM COFACTOR FROM ESCHERICHIA-COLI
AMY, NK
RAJAGOPALAN, KV
[J]. JOURNAL OF BACTERIOLOGY, 1979, 140 (01) : 114 - 124
[3] SITE-DIRECTED MUTAGENESIS OF CONSERVED CYSTEINE RESIDUES WITHIN THE BETA-SUBUNIT OF ESCHERICHIA-COLI NITRATE REDUCTASE - PHYSIOLOGICAL, BIOCHEMICAL, AND EPR CHARACTERIZATION OF THE MUTATED ENZYMES
AUGIER, V
GUIGLIARELLI, B
ASSO, M
BERTRAND, P
FRIXON, C
GIORDANO, G
CHIPPAUX, M
BLASCO, F
[J]. BIOCHEMISTRY, 1993, 32 (08) : 2013 - 2023
[4] REMOVAL OF THE HIGH-POTENTIAL [4FE-4S] CENTER OF THE BETA-SUBUNIT FROM ESCHERICHIA-COLI NITRATE REDUCTASE - PHYSIOLOGICAL, BIOCHEMICAL, AND EPR CHARACTERIZATION OF SITE-DIRECTED MUTATED ENZYMES
AUGIER, V
ASSO, M
GUIGLIARELLI, B
MORE, C
BERTRAND, P
SANTINI, CL
BLASCO, F
CHIPPAUX, M
GIORDANO, G
[J]. BIOCHEMISTRY, 1993, 32 (19) : 5099 - 5108
[5] BERG BL, 1991, J BIOL CHEM, V266, P22380
[6] SEQUENCE-ANALYSIS OF SUBUNITS OF THE MEMBRANE-BOUND NITRATE REDUCTASE FROM A DENITRIFYING BACTERIUM - THE INTEGRAL MEMBRANE SUBUNIT PROVIDES A PROTOTYPE FOR THE DIHEME ELECTRON-CARRYING ARM OF A REDOX LOOP
BERKS, BC
PAGE, MD
RICHARDSON, DJ
REILLY, A
CAVILL, A
OUTEN, F
FERGUSON, SJ
[J]. MOLECULAR MICROBIOLOGY, 1995, 15 (02) : 319 - 331
[7] Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
Berks, BC
Ferguson, SJ
Moir, JWB
Richardson, DJ
[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1995, 1232 (03): : 97 - 173
[8] NUCLEOTIDE-SEQUENCE OF THE DMSABC OPERON ENCODING THE ANAEROBIC DIMETHYLSULFOXIDE REDUCTASE OF ESCHERICHIA-COLI
BILOUS, PT
COLE, ST
ANDERSON, WF
WEINER, JH
[J]. MOLECULAR MICROBIOLOGY, 1988, 2 (06) : 785 - 795
[9] NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli
Blasco, F
Dos Santos, JP
Magalon, A
Frixon, C
Guigliarelli, B
Santini, CL
Giordano, G
[J]. MOLECULAR MICROBIOLOGY, 1998, 28 (03) : 435 - 447
[10] NITRATE REDUCTASE OF ESCHERICHIA-COLI - COMPLETION OF THE NUCLEOTIDE-SEQUENCE OF THE NAR OPERON AND REASSESSMENT OF THE ROLE OF THE ALPHA-SUBUNIT AND BETA-SUBUNIT IN IRON-BINDING AND ELECTRON-TRANSFER
BLASCO, F
IOBBI, C
GIORDANO, G
CHIPPAUX, M
BONNEFOY, V
[J]. MOLECULAR & GENERAL GENETICS, 1989, 218 (02): : 249 - 256

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