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



Gene: narI Accession Numbers: EG10640 (EcoCyc), b1227, ECK1221

Synonyms: chlI

Regulation Summary Diagram: ?

Component of: nitrate reductase A (extended summary available)

Summary:
The γ subunit (NarI) of nitrate reductase A is a membrane-embedded heme-iron subunit resembling cytochrome b, which transfers electrons from the quinone pool to the β subunit (NarH). There are two hemes present, a low-potential heme bL and a high-potential heme bH [Hacket82, Magalon97, Rothery99]. Electrons are thought to transfer from the quinol binding site (Q-site) via heme bL and heme bH to the [3Fe-4S] cluster of NarH [Magalon98, Rothery01]. The Q-site of Nar is periplasmically oriented [Bertero05]. NarI contains 5 transmembrane helices; the first helix appears to facilitate dimer formation. A C-terminal tail interacts with both NarG and NarH. The two Fe atoms are coordinated by histidine groups - His 56 and His 205 coordinate heme bH, His66 and His 187 coordinate heme bL. NarI contains an elongated hydrophobic cavity which may provide a protected interaction site for quinones [Magalon97, Bertero03].

Reviews: [Rothery01a]

Citations: [MacGregor75, Zhao03]

Gene Citations: [Li94a, Darwin96, Bonnefoy97]

Locations: inner membrane

Map Position: [1,285,072 -> 1,285,749] (27.7 centisomes)
Length: 678 bp / 225 aa

Molecular Weight of Polypeptide: 25.497 kD (from nucleotide sequence)

pI: 9.85

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

Unification Links: ASAP:ABE-0004125 , CGSC:458 , DIP:DIP-10313N , EchoBASE:EB0634 , EcoGene:EG10640 , EcoliWiki:b1227 , Mint:MINT-1262739 , ModBase:P11350 , OU-Microarray:b1227 , PortEco:narI , PR:PRO_000023353 , Protein Model Portal:P11350 , RefSeq:NP_415745 , RegulonDB:EG10640 , SMR:P11350 , String:511145.b1227 , UniProt:P11350

Relationship Links: InterPro:IN-FAMILY:IPR003816 , InterPro:IN-FAMILY:IPR023234 , PDB:Structure:1Q16 , 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:PF02665

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Sodergren88]
GO:0042128 - nitrate assimilation Inferred by computational analysis [UniProtGOA11a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0008940 - nitrate reductase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Forget74, Rondeau84, Stewart82]
GO:0009055 - electron carrier activity Inferred from experiment [Bertero03, Rothery99]
GO:0020037 - heme binding Inferred from experiment [Rothery99, Magalon97, Bertero03]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis Inferred from experiment [Bertero03, Berks95]
GO:0009325 - nitrate reductase complex Inferred from experiment Inferred by computational analysis [GOA01a, Sodergren88a]
GO:0044799 - NarGHI complex Inferred from experiment [Bertero03, Forget74]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism biosynthesis of macromolecules (cellular constituents) large molecule carriers cytochromes
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron acceptors

Essentiality data for narI 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:
Revised 03-Aug-2014 by Mackie A , Macquarie University
Last-Curated ? 03-Aug-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 [Berks95a] 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, Rothery01a, 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 [Grove96a].

nar: nitrate reductase [Stewart82]

Reviews: [Blasco01]

Citations: [Fedor14, Garland75, Kristjansson79, Jones80, Morpeth85, vanderOost96, MacGregor75a, MacGregor76, Magalon97a, Rothery01, Rothery98, Magalon98, Grimaldi10, Zhao03a, Grimaldi12, Grimaldi05, Lanciano07, AriasCartin10, Fedor14a, Jones11, Zakian10, Rothery10, Giordani04, Magalon98a, Magalon97, 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, GOA01, GOA01a]
GO:0009055 - electron carrier activity Inferred from experiment [Jones80, 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, GOA01a]
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
Formylation-Modification 1
[UniProt10]
UniProt: N-formylmethionine;
Transmembrane-Region 5 -> 26
[UniProt10, Rothery01a]
UniProt: Helical; Name=1; transmembrane segment 1
Protein-Segment 27 -> 51
[Rothery01a]
cytoplasmic loop
Transmembrane-Region 52 -> 72
[UniProt10, Rothery01a]
UniProt: Helical; Name=2; transmembrane region 2
Metal-Binding-Site 56, 205
[UniProt10, Magalon97, Bertero03]
UniProt: Iron (heme B 1 axial ligand); coordination of high potential heme (heme bH)
Metal-Binding-Site 66, 187
[UniProt10, Magalon97, Bertero03]
UniProt: Iron (heme B 2 axial ligand); coordination of low spin heme (heme bL)
Protein-Segment 73 -> 88
[Rothery01a]
periplasmic loop
Transmembrane-Region 89 -> 109
[UniProt10]
UniProt: Helical; Name=3; transmembrane region 3
Protein-Segment 108 -> 124
[Rothery01a]
periplasmic loop
Transmembrane-Region 125 -> 146
[UniProt10, Rothery01a]
UniProt: Helical; Name=4; transmembrane region 4
Protein-Segment 147 -> 183
[Rothery01a]
periplasmic loop
Transmembrane-Region 184 -> 207
[UniProt10, Rothery01a]
UniProt: Helical; Name=5; transmembrane region 5
Metal-Binding-Site 187
[UniProt10]
UniProt: Iron (heme B 2 axial ligand);
Metal-Binding-Site 205
[UniProt10]
UniProt: Iron (heme B 1 axial ligand);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1227 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10640; 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

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

Berks95: Berks BC, Page MD, Richardson DJ, Reilly A, Cavill A, Outen F, Ferguson SJ (1995). "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." Mol Microbiol 15(2);319-31. PMID: 7746153

Berks95a: 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

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

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

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

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

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

Grove96a: 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

Hacket82: Hacket NR, Bragg PD (1982). "The asociation of two distinct b cytochromes with the respiratory nitrate reductase of Escherichia coli." FEMS Microbiology Letters 13; 213-217.

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

Jones80: 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

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

Li94a: 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). "Anaerobic cytochrome b1 in Escherichia coli: association with and regulation of nitrate reductase." J Bacteriol 121(3);1111-6. PMID: 1090591

MacGregor75a: 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

Magalon97: Magalon A, Lemesle-Meunier D, Rothery RA, Frixon C, Weiner JH, Blasco F (1997). "Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A." J Biol Chem 272(41);25652-8. PMID: 9325288

Magalon97a: Magalon A, Rothery RA, Giordano G, Blasco F, Weiner JH (1997). "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." J Bacteriol 179(16);5037-45. PMID: 9260944

Magalon98: Magalon A, Rothery RA, Lemesle-Meunier D, Frixon C, Weiner JH, Blasco F (1998). "Inhibitor binding within the NarI subunit (cytochrome bnr) of Escherichia coli nitrate reductase A." J Biol Chem 273(18);10851-6. PMID: 9556558

Magalon98a: Magalon A, Asso M, Guigliarelli B, Rothery RA, Bertrand P, Giordano G, Blasco F (1998). "Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit." Biochemistry 37(20);7363-70. PMID: 9585550

Morpeth85: Morpeth FF, Boxer DH (1985). "Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12." Biochemistry 24(1);40-6. PMID: 3888257

Rabin92: Rabin RS, Collins LA, Stewart V (1992). "In vivo requirement of integration host factor for nar (nitrate reductase) operon expression in Escherichia coli K-12." Proc Natl Acad Sci U S A 1992;89(18);8701-5. PMID: 1528882

Rondeau84: Rondeau SS, Hsu PY, DeMoss JA (1984). "Construction in vitro of a cloned nar operon from Escherichia coli." J Bacteriol 159(1);159-66. PMID: 6330027

Rothery01: Rothery RA, Blasco F, Weiner JH (2001). "Electron transfer from heme bL to the [3Fe-4S] cluster of Escherichia coli nitrate reductase A (NarGHI)." Biochemistry 40(17);5260-8. PMID: 11318649

Rothery01a: Rothery RA, Blasco F, Magalon A, Weiner JH (2001). "The diheme cytochrome b subunit (Narl) of Escherichia coli nitrate reductase A (NarGHI): structure, function, and interaction with quinols." J Mol Microbiol Biotechnol 3(2);273-83. PMID: 11321583

Rothery04: Rothery RA, Bertero MG, Cammack R, Palak M, Blasco F, Strynadka NC, Weiner JH (2004). "The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state." Biochemistry 43(18);5324-33. PMID: 15122898

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Rothery99: Rothery RA, Blasco F, Magalon A, Asso M, Weiner JH (1999). "The hemes of Escherichia coli nitrate reductase A (NarGHI): potentiometric effects of inhibitor binding to narI." Biochemistry 1999;38(39);12747-57. PMID: 10504245

RuizHerrera69: Ruiz-Herrera J, DeMoss JA (1969). "Nitrate reductase complex of Escherichia coli K-12: participation of specific formate dehydrogenase and cytochrome b1 components in nitrate reduction." J Bacteriol 99(3);720-9. PMID: 4905536

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Other References Related to Gene Regulation

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Darwin97: Darwin AJ, Tyson KL, Busby SJ, Stewart V (1997). "Differential regulation by the homologous response regulators NarL and NarP of Escherichia coli K-12 depends on DNA binding site arrangement." Mol Microbiol 1997;25(3);583-95. PMID: 9302020

Eiglmeier89: Eiglmeier K, Honore N, Iuchi S, Lin EC, Cole ST (1989). "Molecular genetic analysis of FNR-dependent promoters." Mol Microbiol 1989;3(7);869-78. PMID: 2677602

Lamberg00: Lamberg KE, Kiley PJ (2000). "FNR-dependent activation of the class II dmsA and narG promoters of Escherichia coli requires FNR-activating regions 1 and 3." Mol Microbiol 38(4);817-27. PMID: 11115116

Li88a: Li SF, DeMoss JA (1988). "Location of sequences in the nar promoter of Escherichia coli required for regulation by Fnr and NarL." J Biol Chem 1988;263(27);13700-5. PMID: 3138237

Melville96: Melville SB, Gunsalus RP (1996). "Isolation of an oxygen-sensitive FNR protein of Escherichia coli: interaction at activator and repressor sites of FNR-controlled genes." Proc Natl Acad Sci U S A 93(3);1226-31. PMID: 8577745

Ogasawara07a: Ogasawara H, Hasegawa A, Kanda E, Miki T, Yamamoto K, Ishihama A (2007). "Genomic SELEX search for target promoters under the control of the PhoQP-RstBA signal relay cascade." J Bacteriol 189(13);4791-9. PMID: 17468243

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Rabin93: Rabin RS, Stewart V (1993). "Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12." J Bacteriol 1993;175(11);3259-68. PMID: 8501030

Schroder93: Schroder I, Darie S, Gunsalus RP (1993). "Activation of the Escherichia coli nitrate reductase (narGHJI) operon by NarL and Fnr requires integration host factor." J Biol Chem 268(2);771-4. PMID: 8419352

Stewart82a: Stewart V (1982). "Requirement of Fnr and NarL functions for nitrate reductase expression in Escherichia coli K-12." J Bacteriol 151(3);1320-5. PMID: 7050087

Vine11a: Vine CE, Purewal SK, Cole JA (2011). "NsrR-dependent method for detecting nitric oxide accumulation in the Escherichia coli cytoplasm and enzymes involved in NO production." FEMS Microbiol Lett 325(2);108-14. PMID: 22092912

Walker91: Walker MS, DeMoss JA (1991). "Promoter sequence requirements for Fnr-dependent activation of transcription of the narGHJI operon." Mol Microbiol 5(2);353-60. PMID: 2041473

Zhang96: Zhang X, DeMoss JA (1996). "Structure modification induced in the narG promoter by binding of integration host factor and NARL-P." J Bacteriol 178(13);3971-3. PMID: 8682807


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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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