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Escherichia coli K-12 substr. MG1655 Polypeptide: nitrate reductase A, β subunit



Gene: narH Accession Numbers: EG10639 (EcoCyc), b1225, ECK1219

Synonyms: chlC

Regulation Summary Diagram: ?

Component of: nitrate reductase A (extended summary available)

Summary:
The β subunit (NarH) of nitrate reductase A contains 4 iron-sulfur clusters - one [3Fe-4S] cluster (FS4) and three [4Fe-4S] clusters (FS1, FS2 and FS3) [Johnson85a, Blasco89, Bertero03]. FS1, FS2 and FS3 are coordinated by 4 cysteine residues and FS4 is coordinated by 3 cysteine residues (reviewed by [Blasco01]

nar: nitrate reductase; chl: chlorate resistant [Stewart82]

Citations: [Augier93, Augier93a, Guigliarelli96, Guigliarelli92]

Gene Citations: [Li94b, Darwin96, Bonnefoy97]

Locations: inner membrane

Map Position: [1,282,827 -> 1,284,365] (27.65 centisomes)
Length: 1539 bp / 512 aa

Molecular Weight of Polypeptide: 58.066 kD (from nucleotide sequence)

pI: 5.68

Isozyme Sequence Similarity:
nitrate reductase Z, β subunit: YES

Unification Links: ASAP:ABE-0004121 , CGSC:18118 , DIP:DIP-10312N , EchoBASE:EB0633 , EcoGene:EG10639 , EcoliWiki:b1225 , Mint:MINT-1260007 , ModBase:P11349 , OU-Microarray:b1225 , PortEco:narH , PR:PRO_000023352 , Pride:P11349 , Protein Model Portal:P11349 , RefSeq:NP_415743 , RegulonDB:EG10639 , SMR:P11349 , String:511145.b1225 , UniProt:P11349

Relationship Links: InterPro:IN-FAMILY:IPR006547 , InterPro:IN-FAMILY:IPR017896 , PDB:Structure:1Q16 , PDB:Structure:1R27 , PDB:Structure:1SIW , PDB:Structure:1Y4Z , PDB:Structure:1Y5I , PDB:Structure:1Y5L , PDB:Structure:1Y5N , PDB:Structure:3EGW , PDB:Structure:3IR5 , PDB:Structure:3IR6 , PDB:Structure:3IR7 , Pfam:IN-FAMILY:PF13247 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51379

In Paralogous Gene Group: 223 (21 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Sodergren88]
GO:0042126 - nitrate metabolic process Inferred from experiment Inferred by computational analysis [GOA01, Stewart82]
GO:0042128 - nitrate assimilation Inferred by computational analysis [UniProtGOA11a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Lasserre06, Vergnes06, Banci05, Bertero03, Rothery04, Butland05]
GO:0008940 - nitrate reductase activity Inferred from experiment Inferred by computational analysis [GOA01a, GOA01, Stewart82]
GO:0009055 - electron carrier activity Inferred from experiment [Guigliarelli92]
GO:0051538 - 3 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Johnson85a]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Johnson85a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01, Blasco89]
Cellular Component: GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Lasserre06]
GO:0031224 - intrinsic component of membrane Inferred from experiment [Garland75]
GO:0031235 - intrinsic component of the cytoplasmic side of the plasma membrane Inferred from experiment [Bertero03]
GO:0044799 - NarGHI complex Inferred from experiment [Bertero03, Forget74]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009325 - nitrate reductase complex Inferred by computational analysis [GOA01]

MultiFun Terms: metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron acceptors

Essentiality data for narH knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Curated 28-Apr-2008 by Nolan L , Macquarie University
Last-Curated ? 31-Jul-2014 by Mackie A , Macquarie University


Subunit of: nitrate reductase A

Synonyms: NRA

Subunit composition of nitrate reductase A = [NarG]2[NarH]2[NarI]2
         nitrate reductase A, α subunit = NarG (summary available)
         nitrate reductase A, β subunit = NarH (summary available)
         nitrate reductase A, γ subunit = NarI (extended summary available)

Summary:
narGHI encodes a membrane bound quinol-nitrate oxidoreductase, known as nitrate reductase A (NRA) in E. coli K-12. Nitrate reductase A is a respiratory enzyme that functions as a terminal reductase in electron transport pathways that operate during anaerobic growth in the presence of nitrate (see reviews by [Berks95] and [Unden97]).

The NRA heterotrimer consists of a molybdenum cofactor containing α subunit (NarG), an Fe-S cluster containing β subunit (NarH) and a heme containing γ subunit (NarI) [MacGregor74, Forget74, Clegg76, Enoch75, Sodergren88a]. The redox active prosthetic groups of NRA form an electron transport chain which uses electrons from the membrane quinone pool for the reduction of cytoplasmic nitrate [Bertero03]. Electrons derived from the oxidation of quinol are transferred through two hemes in NarI, one [3Fe-4S] (known as FS4) and three [4Fe-4S] clusters (FS3, FS2 and FS1) in NarH and one [4Fe-4S] (FS0) cluster in NarG to the Mos-bisPGD cofactor where nitrate is reduced to nitrite [Rothery99, Zhao03, Rothery01, Rothery04]

Nitrate reductase A can use both ubiquinol and menaquinol as electron donors [Wissenbach90, Wissenbach92]. Nitrate reductase A has a H+/e- ratio of 1 [Unden97].

A crystal structure of the catalytic and electron transfer subunits (NarG and NarH) has been solved at 2.0 Å resolution [Jormakka04], and structures of the NarGHI complex both alone and in complex with the quinol binding site (Q-site) inhibitor pentachlorophenol have been solved at 1.9 and 2 Å resolution [Bertero03, Bertero05]. NarGH is localised on the cytosolic side of the inner membrane and interacts with the membrane bound NarI subunit through a hydrophobic interface. Eight redox centres form an arc through the centre of the heterotrimer and are suggestive of a pathway for electron transfer from menaquinol to the nitrate reducing site in NarG. NarGHI forms a homodimer in vitro and probably in vivo [Bertero03].

A fourth polypeptide encoded by the narJ gene, is required for the incorporation of the molybdenum cofactor into NarG, the α subunit [Dubourdieu92, Blasco92, Blasco98]. If it is coexpressed with the private chaperone NarJ, the NarGH complex alone is soluble and active with artificial electron donors such as benzyl viologen. NarGH becomes localized to the cytoplasmic side of the inner membrane by interaction with NarI [Blasco92].

Nitrate reductase is responsible for the tellurite reductase activity associated with E. coli membranes. An E. coli strain lacking the membrane associated nitrate reductases is hypersensitive to tellurite under aerobic conditions. A mutant strain which synthesizes nitrate reductase A in large quantities can grow anaereobically with tellurite as the sole electron acceptor. It is not clear whether nitrate reductase is responsible for the total reduction of tellurite to elemental tellurium or whether this reaction is the result of two steps [Avazeri97].

narGHJ and I form an operon in E. coli K-12 which is induced upon anaerobic growth in the presence of nitrate [Sodergren88]. narGHJI is weakly expressed when nitrate levels are low and maximally expressed when nitrate levels are high [Wang99a]

E. coli K-12 contains three nitrate reductases. Two of them, nitrate reductase A (NRA) and nitrate reductase Z (NRZ), are membrane bound and biochemically similar (reviewed in [Bonnefoy94]. The third nitrate reductase, Nap, is located in the periplasm [Grove96].

nar: nitrate reductase [Stewart82]

Reviews: [Blasco01]

Citations: [Fedor14, Garland75, Kristjansson79, Jones80a, Morpeth85, vanderOost96, MacGregor75, MacGregor76, Magalon97, Rothery01a, Rothery98, Magalon98, Grimaldi10, Zhao03a, Grimaldi12, Grimaldi05, Lanciano07, AriasCartin10, Fedor14a, Jones11, Zakian10, Rothery10, Giordani04, Magalon98a, Magalon97a, Tseng94, Rabin92, Guigliarelli92, Vincent78, Vincent79, Blum82]

Locations: inner membrane

Relationship Links: PDB:Structure:1Q16 , PDB:Structure:1SIW , PDB:Structure:1Y4Z , PDB:Structure:1Y5I , PDB:Structure:1Y5L , PDB:Structure:1Y5N

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Li87, Showe68]
GO:0006810 - transport Inferred by computational analysis [GOA00]
Molecular Function: GO:0008940 - nitrate reductase activity Inferred by computational analysis Inferred from experiment [Stewart82, Forget74, Rondeau84, GOA01a, GOA01]
GO:0009055 - electron carrier activity Inferred from experiment [Jones80a, RuizHerrera69]
GO:0048038 - quinone binding Inferred from experiment [Brito95]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment [Clegg76]
GO:0009325 - nitrate reductase complex Inferred by computational analysis Inferred from experiment [Forget74, GOA01]
GO:0031224 - intrinsic component of membrane Inferred from experiment [Garland75]
GO:0031235 - intrinsic component of the cytoplasmic side of the plasma membrane Inferred from experiment [Bertero03]
GO:0044799 - NarGHI complex Inferred from experiment [Bertero03, Forget74]

Credits:
Revised 29-Jul-2014 by Mackie A , Macquarie University
Last-Curated ? 30-Jul-2014 by Mackie A , Macquarie University


Enzymatic reaction of: nitrate reductase

Synonyms: respiratory nitrate reductase, nitrite:(acceptor) oxidoreductase

EC Number: 1.7.5.1

Alternative Substrates for nitrate: chlorate [Forget74 ]

In Pathways: nitrate reduction III (dissimilatory) , nitrate reduction VIII (dissimilatory)

Cofactors or Prosthetic Groups: a [4Fe-4S] iron-sulfur cluster [Comment 5], [3Fe-4S] iron-sulfur cluster , guanylyl molybdenum cofactor

Inhibitors (Competitive): azide [Forget74]

Inhibitors (Unknown Mechanism): 2-n-heptyl-4-hydroxyquinoline-N-oxide [Rothery99] , stigmatellin [Rothery99] , hydrogen cyanide [Forget74]


Enzymatic reaction of: tellurite reductase (nitrate reductase A)

EC Number: 1.97.1.-

tellurite + a reduced electron acceptor <=> Te0 + an oxidized electron acceptor

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Summary:
Tellurite reductase activity was measured using benzyl viologen as an electron donor [Avazeri97]


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 7 -> 35
[UniProt09]
UniProt: 4Fe-4S ferredoxin-type 1;
Metal-Binding-Site 16, 19, 22, 263
[UniProt10a, Blasco01]
UniProt: Iron-sulfur 1 (4Fe-4S); [4Fe-4S] coordination (FS1)
Metal-Binding-Site 19
[UniProt10a]
UniProt: Iron-sulfur 1 (4Fe-4S);
Metal-Binding-Site 22
[UniProt10a]
UniProt: Iron-sulfur 1 (4Fe-4S);
Metal-Binding-Site 26, 244, 247, 259
[UniProt10a, Blasco01]
UniProt: Iron-sulfur 2 (4Fe-4S); [4Fe-4S] coordination (FS2)
Conserved-Region 175 -> 206
[UniProt09]
UniProt: 4Fe-4S ferredoxin-type 2;
Metal-Binding-Site 184, 187, 192, 227
[UniProt10a, Blasco01]
UniProt: Iron-sulfur 3 (4Fe-4S); [4Fe-4S] coordination (FS3)
Metal-Binding-Site 187
[UniProt10a]
UniProt: Iron-sulfur 3 (4Fe-4S);
Metal-Binding-Site 192
[UniProt10a]
UniProt: Iron-sulfur 3 (4Fe-4S);
Metal-Binding-Site 196, 217, 223, 220
[UniProt10a, Blasco01]
UniProt: Iron-sulfur 4 (3Fe-4S); [3Fe-4S] coordination (FS4)
Conserved-Region 208 -> 237
[UniProt09]
UniProt: 4Fe-4S ferredoxin-type 3;
Metal-Binding-Site 217
[UniProt10a]
UniProt: Iron-sulfur 4 (3Fe-4S);
Metal-Binding-Site 223
[UniProt10a]
UniProt: Iron-sulfur 4 (3Fe-4S);
Metal-Binding-Site 227
[UniProt10a]
UniProt: Iron-sulfur 3 (4Fe-4S);
Metal-Binding-Site 244
[UniProt10a]
UniProt: Iron-sulfur 2 (4Fe-4S);
Metal-Binding-Site 247
[UniProt10a]
UniProt: Iron-sulfur 2 (4Fe-4S);
Metal-Binding-Site 259
[UniProt10a]
UniProt: Iron-sulfur 2 (4Fe-4S);
Metal-Binding-Site 263
[UniProt10a]
UniProt: Iron-sulfur 1 (4Fe-4S);
Sequence-Conflict 398 -> 417
[Sodergren88, UniProt10a]
Alternate sequence: DTKPVLRALKRMLAMRHYKR → EYQTGTARTETYAGDASLQT; UniProt: (in Ref. 6; AAA24195);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1225 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10639; confirmed by SwissProt match.


References

AriasCartin10: Arias-Cartin R, Lyubenova S, Ceccaldi P, Prisner T, Magalon A, Guigliarelli B, Grimaldi S (2010). "HYSCORE evidence that endogenous mena- and ubisemiquinone bind at the same Q site (Q(D)) of Escherichia coli nitrate reductase A." J Am Chem Soc 132(17);5942-3. PMID: 20387886

Augier93: Augier V, Guigliarelli B, Asso M, Bertrand P, Frixon C, Giordano G, Chippaux M, Blasco F (1993). "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." Biochemistry 32(8);2013-23. PMID: 8383531

Augier93a: Augier V, Asso M, Guigliarelli B, More C, Bertrand P, Santini CL, Blasco F, Chippaux M, Giordano G (1993). "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." Biochemistry 32(19);5099-108. PMID: 8388253

Avazeri97: Avazeri C, Turner RJ, Pommier J, Weiner JH, Giordano G, Vermeglio A (1997). "Tellurite reductase activity of nitrate reductase is responsible for the basal resistance of Escherichia coli to tellurite." Microbiology 143 ( Pt 4);1181-9. PMID: 9141681

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Banci05: Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A (2005). "An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein." FEBS J 272(3);865-71. PMID: 15670166

Berks95: Berks BC, Ferguson SJ, Moir JW, Richardson DJ (1995). "Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions." Biochim Biophys Acta 1232(3);97-173. PMID: 8534676

Bertero03: Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC (2003). "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A." Nat Struct Biol 10(9);681-7. PMID: 12910261

Bertero05: Bertero MG, Rothery RA, Boroumand N, Palak M, Blasco F, Ginet N, Weiner JH, Strynadka NC (2005). "Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A." J Biol Chem 280(15);14836-43. PMID: 15615728

Blasco01: Blasco F, Guigliarelli B, Magalon A, Asso M, Giordano G, Rothery RA (2001). "The coordination and function of the redox centres of the membrane-bound nitrate reductases." Cell Mol Life Sci 58(2);179-93. PMID: 11289300

Blasco89: Blasco F, Iobbi C, Giordano G, Chippaux M, Bonnefoy V (1989). "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." Mol Gen Genet 218(2);249-56. PMID: 2674654

Blasco92: Blasco F, Pommier J, Augier V, Chippaux M, Giordano G (1992). "Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli." Mol Microbiol 1992;6(2);221-30. PMID: 1545706

Blasco98: Blasco F, Dos Santos JP, Magalon A, Frixon C, Guigliarelli B, Santini CL, Giordano G (1998). "NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli." Mol Microbiol 28(3);435-47. PMID: 9632249

Blum82: Blum H, Poole RK (1982). "The molybdenum and iron-sulphur centres of Escherichia coli nitrate reductase are non-randomly oriented in the membrane." Biochem Biophys Res Commun 107(3);903-9. PMID: 6291520

Bonnefoy94: Bonnefoy V, Demoss JA (1994). "Nitrate reductases in Escherichia coli." Antonie Van Leeuwenhoek 1994;66(1-3);47-56. PMID: 7747940

Bonnefoy97: Bonnefoy V, Ratouchniak J, Blasco F, Chippaux M (1997). "Organization of the nar genes at the chlZ locus." FEMS Microbiol Lett 1997;147(1);147-9. PMID: 9037773

Brito95: Brito F, DeMoss JA, Dubourdieu M (1995). "Isolation and identification of menaquinone-9 from purified nitrate reductase of Escherichia coli." J Bacteriol 177(13);3728-35. PMID: 7601837

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Clegg76: Clegg RA (1976). "Purification and some properties of nitrate reductase (EC 1.7.99.4) from Escherichia coli K12." Biochem J 153(3);533-41. PMID: 782444

Darwin96: Darwin AJ, Li J, Stewart V (1996). "Analysis of nitrate regulatory protein NarL-binding sites in the fdnG and narG operon control regions of Escherichia coli K-12." Mol Microbiol 1996;20(3);621-32. PMID: 8736541

Dubourdieu92: Dubourdieu M, DeMoss JA (1992). "The narJ gene product is required for biogenesis of respiratory nitrate reductase in Escherichia coli." J Bacteriol 1992;174(3);867-72. PMID: 1732220

Enoch75: Enoch HG, Lester RL (1975). "The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli." J Biol Chem 1975;250(17);6693-705. PMID: 1099093

Fedor14: Fedor JG, Rothery RA, Weiner JH (2014). "A New Paradigm for Electron Transfer through Escherichia coli Nitrate Reductase A." Biochemistry 53(28);4549-56. PMID: 24960296

Fedor14a: Fedor JG, Rothery RA, Giraldi KS, Weiner JH (2014). "Q-site occupancy defines heme heterogeneity in Escherichia coli nitrate reductase A (NarGHI)." Biochemistry 53(11);1733-41. PMID: 24592999

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Forget74: Forget P (1974). "The bacterial nitrate reductases. Solubilization, purification and properties of the enzyme A of Escherichia coli K 12." Eur J Biochem 1974;42(2);325-32. PMID: 4151408

Garland75: Garland PB, Downie JA, Haddock BA (1975). "Proton translocation and the respiratory nitrate reductase of Escherichia coli." Biochem J 152(3);547-59. PMID: 5996

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Giordani04: Giordani R, Buc J (2004). "Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli." Eur J Biochem 271(12);2400-7. PMID: 15182355

GOA00: GOA (2000). "Gene Ontology annotation based on Swiss-Prot keyword mapping."

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Grimaldi05: Grimaldi S, Lanciano P, Bertrand P, Blasco F, Guigliarelli B (2005). "Evidence for an EPR-detectable semiquinone intermediate stabilized in the membrane-bound subunit NarI of nitrate reductase A (NarGHI) from Escherichia coli." Biochemistry 44(4);1300-8. PMID: 15667223

Grimaldi10: Grimaldi S, Arias-Cartin R, Lanciano P, Lyubenova S, Endeward B, Prisner TF, Magalon A, Guigliarelli B (2010). "Direct evidence for nitrogen ligation to the high stability semiquinone intermediate in Escherichia coli nitrate reductase A." J Biol Chem 285(1);179-87. PMID: 19892705

Grimaldi12: Grimaldi S, Arias-Cartin R, Lanciano P, Lyubenova S, Szenes R, Endeward B, Prisner TF, Guigliarelli B, Magalon A (2012). "Determination of the proton environment of high stability Menasemiquinone intermediate in Escherichia coli nitrate reductase A by pulsed EPR." J Biol Chem 287(7);4662-70. PMID: 22190684

Grove96: Grove J, Tanapongpipat S, Thomas G, Griffiths L, Crooke H, Cole J (1996). "Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm." Mol Microbiol 1996;19(3);467-81. PMID: 8830238

Guigliarelli92: Guigliarelli B, Asso M, More C, Augier V, Blasco F, Pommier J, Giordano G, Bertrand P (1992). "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." Eur J Biochem 207(1);61-8. PMID: 1321049

Guigliarelli96: Guigliarelli B, Magalon A, Asso M, Bertrand P, Frixon C, Giordano G, Blasco F (1996). "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." Biochemistry 35(15);4828-36. PMID: 8664273

Johnson85a: Johnson MK, Bennett DE, Morningstar JE, Adams MW, Mortenson LE (1985). "The iron-sulfur cluster composition of Escherichia coli nitrate reductase." J Biol Chem 260(9);5456-63. PMID: 2985594

Jones11: Jones SA, Gibson T, Maltby RC, Chowdhury FZ, Stewart V, Cohen PS, Conway T (2011). "Anaerobic Respiration of Escherichia coli in the Mouse Intestine." Infect Immun 79(10);4218-26. PMID: 21825069

Jones80a: Jones RW, Lamont A, Garland PB (1980). "The mechanism of proton translocation driven by the respiratory nitrate reductase complex of Escherichia coli." Biochem J 190(1);79-94. PMID: 6255943

Jormakka04: Jormakka M, Richardson D, Byrne B, Iwata S (2004). "Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes." Structure (Camb) 12(1);95-104. PMID: 14725769

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kristjansson79: Kristjansson JK, Hollocher TC (1979). "Substrate binding site for nitrate reductase of Escherichia coli is on the inner aspect of the membrane." J Bacteriol 137(3);1227-33. PMID: 374343

Lanciano07: Lanciano P, Magalon A, Bertrand P, Guigliarelli B, Grimaldi S (2007). "High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD." Biochemistry 46(18);5323-9. PMID: 17439244

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Li87: Li SF, DeMoss JA (1987). "Promoter region of the nar operon of Escherichia coli: nucleotide sequence and transcription initiation signals." J Bacteriol 169(10);4614-20. PMID: 3308846

Li94b: Li J, Kustu S, Stewart V (1994). "In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK and frdA operon control regions of Escherichia coli K-12." J Mol Biol 1994;241(2);150-65. PMID: 8057356

MacGregor74: MacGregor CH, Schnaitman CA, Normansell DE (1974). "Purification and properties of nitrate reductase from Escherichia coli K12." J Biol Chem 249(16);5321-7. PMID: 4137146

MacGregor75: MacGregor CH (1975). "Solubilization of Escherichia coli nitrate reductase by a membrane-bound protease." J Bacteriol 121(3);1102-10. PMID: 1090590

MacGregor76: MacGregor CH (1976). "Biosynthesis of membrane-bound nitrate reductase in Escherichia coli: evidence for a soluble precursor." J Bacteriol 126(1);122-31. PMID: 770417

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Other References Related to Gene Regulation

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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