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

Cellular and Molecular Life Sciences

Volumn 58, Issue 2, 2001, Pages 179-193

  Blasco, F ^a   Guigliarelli, B ^b   Magalon, A ^a   Asso, M ^b   Giordano, G ^a   Rothery, R A ^c  

^a AIX MARSEILLE UNIVERSITÉ   (France)

^b AIX MARSEILLE UNIVERSITÉ   (France)

^c UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Haems; Molybdenum cofactor; Nitrate reductase; Fe S centres

Indexed keywords

MOLYBDENUM COMPLEX; NITRATE REDUCTASE;

ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME SUBUNIT; ESCHERICHIA COLI; NITRIFICATION; NONHUMAN; OXIDATION REDUCTION REACTION; REVIEW; STRUCTURE ACTIVITY RELATION;

ESCHERICHIA COLI;

EID: 0035102909     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00000846     Document Type: Review

References (95)

1. Nitrate reductase of Escherichia coli: Completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron-transfer
2. Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm
3. Nitrate reductases of Escherichia coli: Sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon
4. Nitrate reductases in Escherichia coli
5. Biochemical and immunological evidence for a second nitrate reductase in Escherichia coli K12
6. Expression of the Escherichia coli NRZ nitrate reductase is highly growth phase dependent and is controlled by RpoS, the alternative vegetative sigma factor
7. Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12
8. Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: Does Nap confer a selective advantage during nitrate-limited growth?
9. The napF and narG nitrate reductase operons in Escherichia coli are differentially expressed in response to submicromolar concentrations of nitrate but not nitrite
10. Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
11. Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution
12. Crystal structure of formate dehydrogenase H: Catalysis involving Mo, molybdoprotein, selenocysteine and an Fe4S4 cluster
13. Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 Å resolution
14. Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods
15. Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
16. Enzymes depending on the pterin molybdenum cofactor: Sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains
17. Engineering a novel iron-sulfur cluster into the catalytic subunit of Escherichia coli dimethyl-sulfoxide reductase
18. Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas
19. Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: Investigation by site-directed mutagenesis of the conserved is-50 residue in the NarG subunit
20. Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase
21. Multiple pathways of electron-transfer in dimethyl sulfoxide reductase of Escherichia coli
22. The mononuclear molybdenum enzymes
23. Electron-paramagnetic-resonance studies on nitrate reductase from Escherichia coli K12
24. Electron-paramagnetic-resonance spectroscopy studies on the dissimilatory nitrate reductase from Pseudomonas aeruginosa
25. Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli
26. Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli
27. Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli
28. NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli
29. The anaerobic life of Bacillus subtilis: Cloning of the genes encoding the respiratory nitrate reductase system
30. A thermophilic nitrate reductase is responsible for the strain specific anaerobic growth of Thermus thermophilus HB8
31. Characterization of NarJ, a system-specific chaperone required for nitrate reductase biogenesis in Escherichia coli
32. The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters
33. Characterization of molybdenum cofactor from Escherichia coli
34. Involvement of a protein with molybdenum cofactor in the in vitro activation of nitrate reductase from a chlA mutant of Escherichia coli K12
35. In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly
36. Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation
37. TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli
38. Role of XdhC in molybdenum cofactor insertion into xanthine dehydrogenase of Rhodobacter capsulatus
39. Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine
40. Nucelotide sequence of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase of Escherichia coli
41. Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes
42. Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulphide reductase
43. EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism
44. A new approach for the structural study of metalloproteins: The quantitative analysis of intercenter magnetic interactions
45. 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
46. Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters
47. 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
48. 7-iron ferredoxin revisited
49. Application of EPR spectroscopy to the structural and functional study of iron-sulfur proteins
50. Modified ligands to FA and FB in photosystem I. I. Structural constraints for the formation of iron-sulfur clusters in free and rebound PsaC
51. A comparative analysis of the spin state distribution of in vitro and in vivo mutant of PsaC
52. Characterization by electron paramagnetic resonance of the role of the Escherichia coli nitrate reductase (NarGHI) iron-sulfur clusters in electron-transfer to nitrate and identification of a semiquinone radical intermediate
53. Dissimilatory nitrate reductase in bacteria
54. Structure of Escherichia coli fumarate reductase respiratory complex
55. Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution
56. [3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans [NiFe] hydrogenase by site-directed mutagenesis
57. Natural engineering principles of electron tunnelling in biological oxidation-reduction
58. Heme axial ligation by the highly conserved His residues in helix II of cytochrone b (NarI) of Escherichia coli nitrate reductase A
59. The association of two distinct b cytochromes with the respiratory nitrate reductase of Escherichia coli
60. The hemes of Escherichia coli nitrate reductase A (NarGHI): Potentiometric effects of inhibitor binding to NarI
61. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
62. Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: The integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop
63. Inhibitor binding within the NarI subunit (cytochrome bnr) of Escherichia coli nitrate reductase A
64. Escherichia coli fumarate reductase frdC and frdD mutants. Identification of amino acid residues involved in catalytic activity with quinones
65. Models for structure and function in quinone binding sites: The Escherichia coli quinol oxidase, cytochrome bo3
66. Models of the cytochromes b. Effect of axial ligand plane orientation on the EPR and Mossbauer spectra of low-spin ferrihemes
67. Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64→Val/Va168→ His double mutant
68. Cytochrome electron spin resonance line, ligand fields and components stoichiometry in ubiquinol-cytochrome c oxidoreductase
69. Isolation and characterization of a two-subunit cytochrome bc1 subcomplex from Rhodobacter capsulatus and reconstitution of its ubihydroquinone oxidation (Qo) site with purified Fe-S protein subunit
70. Electron-transfer by domain movement in cytochrome bc1
71. Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria
72. Electrochemical and spectral analysis of the long-range interactions between the Qo and Qi sites and the heme prosthetic groups in ubiquinolcytochrome c oxidoreductase
73. 1 complex from Rhodobacter sphaeroides by site-directed mutagenesis
74. Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis
75. Topological characterization of Escherichia coli DMSO reductase by electron paramagnetic resonance spectroscopy of an engineered [3Fe-4S] cluster
76. Interaction of an engineered [3Fe-4S] cluster with a menaquinol binding site of Escherichia coli DMSO reductase
77. Properties of bovine heart mitochondrial cytochrome b560
78. Resolution and reconstitution of succinate-ubiquinone reductase from Escherichia coli
79. The redox properties of cytochromes b imposed by the membrane electrostatic environment
80. Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA- menA- double quinone mutant
81. Hydroxylated naphthoquinones as substrates for Escherichia coli anaerobic reductases
82. Analysis of inhibitor binding to the mitochondrial cytochrome c reductase by fluorescence quench titration. Evidence for a 'catalytic switch' at the Qo center
83. Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
84. Binding of HOQNO to beef-heart submitochondrial particles
85. The mechanism of proton translocation driven by the respiratory nitrate reductase complex of Escherichia coli
86. Isolation and identification of menaquinone-9 from purified nitrate reductase of Escherichia coli
87. Interaction of a menaquinol binding site with the [3Fe-4S] cluster of Escherichia coli fumarate reductase
88. An Escherichia coli mutant quinol: Fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone binding site
89. Kinetic studies of membrane-bound nitrate reductase A from Escherichia coli with menadiol and duroquinol, analogues of physiological electron donors
90. Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12
91. Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo
92. Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli
93. Stabilization of a semiquinone radical at the high-affinity quinone binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase
94. Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides
95. Photosynthetic reaction centers