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Escherichia coli K-12 substr. MG1655 Enzyme: nitric oxide dioxygenase



Gene: hmp Accession Numbers: EG10456 (EcoCyc), b2552, ECK2549

Synonyms: fsrB, hmpA, flavohemoglobin, flavohemoprotein

Regulation Summary Diagram: ?

Summary:
Hmp is a flavohemoglobin [Ioannidis92] with multiple enzymatic activities; however, its nitric oxide dioxygenase (NOD) activity appears to be the physiologically relevant function [Gardner98]. Under aerobic conditions, Hmp detoxifies nitric oxide (NO) and thus protects the respiratory cytochromes bo' or bd [Hausladen98, Stevanin00, Gardner02a]. NO tolerance is correlated with virulence [Svensson06] and survival in macrophages [Stevanin07].

The nitric oxide dioxygenase reaction appears to occur in two steps. First, NAD(P)H reduces the bound FAD, which then reduces the heme iron. O2 then binds to the reduced flavohemoglobin, which dioxygenates NO, forming nitrate [Gardner00]. However, heme ligand turnover and NADH consumption at different O2/NO concentrations suggests that the enzyme binds NO first; the nitroxyl equivalent is then oxidized [Hausladen01]. The reaction mechanism has been investigated further [Gardner06].

The steric and dielectric environment of the heme iron has been investigated [Bonamore01]. The active site structure appears to be similar to that of peroxidases [Mukai01]. A crystal structure of Hmp has been solved at 2.2 Å resolution, showing that the N-terminal globin domain, central FAD-binding domain, and C-terminal NADH-binding domain are arranged in a heart-shaped structure [Ilari02a]. All domains are required for Hmp function [HernandezUrzua03]. Folding of the globin domain has been studied [Eun08].

Hmp activity causes oxidative stress in the cell due to production of superoxide by its NADH oxidase activity [MembrilloHernan96, Poole94, Poole96, Wu04a]. Hmp can oxidize both NADH and NADPH with a Km of 1.8 and 19.6 µM, respectively [Anjum98].

The ferrisiderophore reductase activity [Andrews92] and ferric citrate reductase activity [MembrilloHernan96] of Hmp is a result of the flavin reductase activity of Hmp [Eschenbrenner94]. Hmp was also shown to have dihydropteridine reductase [Vasudevan91], cytochrome c reductase and ferric hydroxamate reductase [Poole97] as well as alkylhydroperoxide reductase activity [Bonamore03].

Hmp binds unsaturated or cyclopropanated fatty acids [Bonamore03a, DAngelo04].

The enzyme is inhibited by the imidazole class of antibiotics, including miconazole and econazole [Helmick05].

Expression of hmp is regulated in response to oxygen, nitrogen compounds, and iron availability [Poole96a, Flatley05] and is induced by acid [Yohannes04]. NO induction is mediated by Fnr [CruzRamos02] and Fur [DAutreaux02]. An hmp mutant is more sensitive to nitric oxide than wild type [Gardner98, Hausladen98, MembrilloHernan99b], but has a growth advantage in mixed cultures [Stevanin07]. The rate of NO reduction in anaerobically grown cells appears to be unaffected in an hmp mutant [Vine11a].

Hmp: "haemoprotein" [Vasudevan91]

FsrB: "ferrisiderophore reductase B" [Andrews92]

Reviews: [Poole00, Gardner05, Poole05, Spiro06, Lewis08a, Bonamore08]

Citations: [Orii92, Liu93d, Cooper94, Vasudevan95]

Locations: periplasmic space, cytosol

Map Position: [2,683,857 -> 2,685,047] (57.85 centisomes)
Length: 1191 bp / 396 aa

Molecular Weight of Polypeptide: 43.868 kD (from nucleotide sequence), 44.0 kD (experimental) [Vasudevan91 ]

pI: 5.77

Unification Links: ASAP:ABE-0008396 , EchoBASE:EB0451 , EcoGene:EG10456 , EcoliWiki:b2552 , ModBase:P24232 , OU-Microarray:b2552 , PortEco:hmp , PR:PRO_000022907 , Pride:P24232 , Protein Model Portal:P24232 , RefSeq:NP_417047 , RegulonDB:EG10456 , SMR:P24232 , String:511145.b2552 , UniProt:P24232

Relationship Links: InterPro:IN-FAMILY:IPR000971 , InterPro:IN-FAMILY:IPR001221 , InterPro:IN-FAMILY:IPR001433 , InterPro:IN-FAMILY:IPR008333 , InterPro:IN-FAMILY:IPR009050 , InterPro:IN-FAMILY:IPR012292 , InterPro:IN-FAMILY:IPR017927 , InterPro:IN-FAMILY:IPR017938 , InterPro:IN-FAMILY:IPR023950 , PDB:Structure:1GVH , Pfam:IN-FAMILY:PF00042 , Pfam:IN-FAMILY:PF00175 , Pfam:IN-FAMILY:PF00970 , Prints:IN-FAMILY:PR00410 , Prosite:IN-FAMILY:PS01033 , Prosite:IN-FAMILY:PS51384

In Paralogous Gene Group: 219 (6 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0051409 - response to nitrosative stress Inferred from experiment Inferred by computational analysis [GOA01, MembrilloHernan99b, Gardner98a, Poole96a]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0009636 - response to toxic substance Inferred by computational analysis [UniProtGOA11a]
GO:0015671 - oxygen transport Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0005504 - fatty acid binding Inferred from experiment [Bonamore03a]
GO:0008941 - nitric oxide dioxygenase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Gardner00, Gardner98]
GO:0020037 - heme binding Inferred from experiment Inferred by computational analysis [GOA01, Vasudevan91, Ioannidis92]
GO:0032843 - hydroperoxide reductase activity Inferred from experiment [Bonamore03]
GO:0071949 - FAD binding Inferred from experiment Inferred by computational analysis [GOA01, Ioannidis92]
GO:0005344 - oxygen transporter activity Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0005506 - iron ion binding Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0019825 - oxygen binding Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism central intermediary metabolism unassigned reversible reactions

Essentiality data for hmp 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:
Last-Curated ? 25-Oct-2011 by Keseler I , SRI International


Enzymatic reaction of: nitric oxide dioxygenase

Synonyms: NOD

EC Number: 1.14.12.17

2 nitric oxide + NAD(P)H + 2 oxygen <=> 2 nitrate + NAD(P)+ + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Citations: [Kim99f, Gardner08]

Cofactors or Prosthetic Groups: protoheme IX [Ioannidis92], FAD [Gardner00, Ioannidis92]

Inhibitors (Unknown Mechanism): miconazole [Helmick05] , hydrogen cyanide [Gardner98, Stevanin00]

Kinetic Parameters:

Substrate
Km (μM)
Citations
oxygen
100.0
[Gardner00]
NAD(P)H
4.8
[Gardner00]
nitric oxide
0.28
[Gardner00]

T(opt): 37 °C [Gardner00]


Enzymatic reaction of: dihydropteridine reductase (nitric oxide dioxygenase)

Synonyms: NAD(P)H:6,7-dihydropteridine oxidoreductase

EC Number: 1.5.1.34

a 5,6,7,8-tetrahydropteridine + NAD(P)+ <=> a 6,7-dihydropteridine + NAD(P)H + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

Cofactors or Prosthetic Groups: protoheme IX [Ioannidis92], FAD [Ioannidis92]


Sequence Features

Feature Class Location Citations Comment
Protein-Segment 1 -> 138
[UniProt10a]
UniProt: Globin; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 29
[Gardner00, UniProt11]
Alternate sequence: Y → F; UniProt: 30-fold reduction in NO dioxygenase activity, and 80-fold increase in the O(2) dissociation rate constant.
Alternate sequence: Y → H; UniProt: 15 to 35-fold reduction in NO dioxygenase activity.
Alternate sequence: Y → E; UniProt: 15 to 35-fold reduction in NO dioxygenase activity.
Amino-Acid-Site 29
[UniProt10]
UniProt: Involved in heme-bound ligand stabilization and O-O bond activation; Sequence Annotation Type: site;
Amino-Acid-Site 84
[UniProt10]
UniProt: Influences the redox potential of the prosthetic heme and FAD groups; Sequence Annotation Type: site;
Metal-Binding-Site 85
[UniProt10]
UniProt: Iron (heme proximal ligand);
Active-Site 95
[Mukai01, UniProt11]
UniProt: Charge relay system.
Active-Site 135
[Mukai01, UniProt11]
UniProt: Charge relay system.
Protein-Segment 147 -> 396
[UniProt10a]
UniProt: Reductase; Sequence Annotation Type: region of interest;
Conserved-Region 150 -> 255
[UniProt09]
UniProt: FAD-binding FR-type;
Amino-Acid-Sites-That-Bind 188
[UniProt10]
UniProt: FAD;
Nucleotide-Phosphate-Binding-Region 204 -> 207
[UniProt10]
UniProt: FAD;
Protein-Segment 259 -> 396
[UniProt10a]
UniProt: NAD or NADP-binding; Sequence Annotation Type: region of interest;
Nucleotide-Phosphate-Binding-Region 268 -> 273
[UniProt10a]
UniProt: NADP; Non-Experimental Qualifier: by similarity;
Amino-Acid-Site 388
[UniProt10]
UniProt: Influences the redox potential of the prosthetic heme and FAD groups; Sequence Annotation Type: site;
Nucleotide-Phosphate-Binding-Region 389 -> 392
[UniProt10]
UniProt: FAD;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
3/2/1998 (pkarp) Merged genes G679/EG10456 and EG10456/hmpA
1/26/1998 (pkarp) Merged genes G7985/hmpA and EG10456/hmp


References

Andrews92: Andrews SC, Shipley D, Keen JN, Findlay JB, Harrison PM, Guest JR (1992). "The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases." FEBS Lett 1992;302(3);247-52. PMID: 1601132

Anjum98: Anjum MF, Ioannidis N, Poole RK (1998). "Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged oxidative stress and implications for its physiological role in Escherichia coli." FEMS Microbiol Lett 166(2);219-23. PMID: 9770277

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

Bonamore01: Bonamore A, Chiancone E, Boffi A (2001). "The distal heme pocket of Escherichia coli flavohemoglobin probed by infrared spectroscopy." Biochim Biophys Acta 1549(2);174-8. PMID: 11690654

Bonamore03: Bonamore A, Gentili P, Ilari A, Schinina ME, Boffi A (2003). "Escherichia coli flavohemoglobin is an efficient alkylhydroperoxide reductase." J Biol Chem 278(25);22272-7. PMID: 12663656

Bonamore03a: Bonamore A, Farina A, Gattoni M, Schinina ME, Bellelli A, Boffi A (2003). "Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin." Biochemistry 42(19);5792-801. PMID: 12741837

Bonamore08: Bonamore A, Boffi A (2008). "Flavohemoglobin: structure and reactivity." IUBMB Life 60(1);19-28. PMID: 18379989

Cooper94: Cooper CE, Ioannidis N, D'mello R, Poole RK (1994). "Haem, flavin and oxygen interactions in Hmp, a flavohaemoglobin from Escherichia coli." Biochem Soc Trans 1994;22(3);709-13. PMID: 7821669

CruzRamos02: Cruz-Ramos H, Crack J, Wu G, Hughes MN, Scott C, Thomson AJ, Green J, Poole RK (2002). "NO sensing by FNR: regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp." EMBO J 21(13);3235-44. PMID: 12093725

DAngelo04: D'Angelo P, Lucarelli D, della Longa S, Benfatto M, Hazemann JL, Feis A, Smulevich G, Ilari A, Bonamore A, Boffi A (2004). "Unusual heme iron-lipid acyl chain coordination in Escherichia coli flavohemoglobin." Biophys J 86(6);3882-92. PMID: 15189885

DAutreaux02: D'Autreaux B, Touati D, Bersch B, Latour JM, Michaud-Soret I (2002). "Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron." Proc Natl Acad Sci U S A 99(26);16619-24. PMID: 12475930

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

Eschenbrenner94: Eschenbrenner M, Coves J, Fontecave M (1994). "Ferric reductases in Escherichia coli: the contribution of the haemoglobin-like protein." Biochem Biophys Res Commun 1994;198(1);127-31. PMID: 8292013

Eun08: Eun YJ, Kurt N, Sekhar A, Cavagnero S (2008). "Thermodynamic and kinetic characterization of apoHmpH, a fast-folding bacterial globin." J Mol Biol 376(3);879-97. PMID: 18187151

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

Flatley05: Flatley J, Barrett J, Pullan ST, Hughes MN, Green J, Poole RK (2005). "Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis." J Biol Chem 280(11);10065-72. PMID: 15647275

Gardner00: Gardner AM, Martin LA, Gardner PR, Dou Y, Olson JS (2000). "Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis." J Biol Chem 2000;275(17);12581-9. PMID: 10777548

Gardner00a: Gardner PR, Gardner AM, Martin LA, Dou Y, Li T, Olson JS, Zhu H, Riggs AF (2000). "Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon monoxide inhibition." J Biol Chem 275(41);31581-7. PMID: 10922365

Gardner02a: Gardner AM, Gardner PR (2002). "Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity." J Biol Chem 277(10);8166-71. PMID: 11751864

Gardner05: Gardner PR (2005). "Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases." J Inorg Biochem 99(1);247-66. PMID: 15598505

Gardner06: Gardner PR, Gardner AM, Brashear WT, Suzuki T, Hvitved AN, Setchell KD, Olson JS (2006). "Hemoglobins dioxygenate nitric oxide with high fidelity." J Inorg Biochem 100(4);542-50. PMID: 16439024

Gardner08: Gardner PR (2008). "Assay and characterization of the NO dioxygenase activity of flavohemoglobins." Methods Enzymol 436;217-37. PMID: 18237635

Gardner98: Gardner PR, Gardner AM, Martin LA, Salzman AL (1998). "Nitric oxide dioxygenase: an enzymic function for flavohemoglobin." Proc Natl Acad Sci U S A 1998;95(18);10378-83. PMID: 9724711

Gardner98a: Gardner PR, Costantino G, Salzman AL (1998). "Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase." J Biol Chem 273(41);26528-33. PMID: 9756889

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

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.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Hausladen01: Hausladen A, Gow A, Stamler JS (2001). "Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen." Proc Natl Acad Sci U S A 98(18);10108-12. PMID: 11517313

Hausladen98: Hausladen A, Gow AJ, Stamler JS (1998). "Nitrosative stress: metabolic pathway involving the flavohemoglobin." Proc Natl Acad Sci U S A 95(24);14100-5. PMID: 9826660

Helmick05: Helmick RA, Fletcher AE, Gardner AM, Gessner CR, Hvitved AN, Gustin MC, Gardner PR (2005). "Imidazole antibiotics inhibit the nitric oxide dioxygenase function of microbial flavohemoglobin." Antimicrob Agents Chemother 49(5);1837-43. PMID: 15855504

HernandezUrzua03: Hernandez-Urzua E, Mills CE, White GP, Contreras-Zentella ML, Escamilla E, Vasudevan SG, Membrillo-Hernandez J, Poole RK (2003). "Flavohemoglobin Hmp, but not its individual domains, confers protection from respiratory inhibition by nitric oxide in Escherichia coli." J Biol Chem 278(37);34975-82. PMID: 12826671

Ilari02a: Ilari A, Bonamore A, Farina A, Johnson KA, Boffi A (2002). "The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket." J Biol Chem 277(26);23725-32. PMID: 11964402

Ioannidis92: Ioannidis N, Cooper CE, Poole RK (1992). "Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli." Biochem J 1992;288 ( Pt 2);649-55. PMID: 1334413

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

Kim99f: Kim SO, Orii Y, Lloyd D, Hughes MN, Poole RK (1999). "Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): reversible binding of nitric oxide and reduction to nitrous oxide." FEBS Lett 445(2-3);389-94. PMID: 10094495

Lewis08a: Lewis ME, Corker HA, Gollan B, Poole RK (2008). "A survey of methods for the purification of microbial flavohemoglobins." Methods Enzymol 436;169-86. PMID: 18237632

Liu93d: Liu J, Magasanik B (1993). "The glnB region of the Escherichia coli chromosome." J Bacteriol 1993;175(22);7441-9. PMID: 8226691

MembrilloHernan96: Membrillo-Hernandez J, Ioannidis N, Poole RK (1996). "The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo." FEBS Lett 1996;382(1-2);141-4. PMID: 8612736

MembrilloHernan97: Membrillo-Hernandez J, Cook GM, Poole RK (1997). "Roles of RpoS (sigmaS), IHF and ppGpp in the expression of the hmp gene encoding the flavohemoglobin (Hmp) of Escherichia coli K-12." Mol Gen Genet 1997;254(5);599-603. PMID: 9197421

MembrilloHernan99b: Membrillo-Hernandez J, Coopamah MD, Anjum MF, Stevanin TM, Kelly A, Hughes MN, Poole RK (1999). "The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a "Nitric oxide Releaser," and paraquat and is essential for transcriptional responses to oxidative stress." J Biol Chem 274(2);748-54. PMID: 9873011

Mills01: Mills CE, Sedelnikova S, Soballe B, Hughes MN, Poole RK (2001). "Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide." Biochem J 353(Pt 2);207-13. PMID: 11139382

Mukai01: Mukai M, Mills CE, Poole RK, Yeh SR (2001). "Flavohemoglobin, a globin with a peroxidase-like catalytic site." J Biol Chem 276(10);7272-7. PMID: 11092893

Orii92: Orii Y, Ioannidis N, Poole RK (1992). "The oxygenated flavohaemoglobin from Escherichia coli: evidence from photodissociation and rapid-scan studies for two kinetic and spectral forms." Biochem Biophys Res Commun 1992;187(1);94-100. PMID: 1325799

Plamann83: Plamann MD, Stauffer GV (1983). "Characterization of the Escherichia coli gene for serine hydroxymethyltransferase." Gene 22(1);9-18. PMID: 6190704

Poole00: Poole RK, Hughes MN (2000). "New functions for the ancient globin family: bacterial responses to nitric oxide and nitrosative stress." Mol Microbiol 36(4);775-83. PMID: 10844666

Poole05: Poole RK (2005). "Nitric oxide and nitrosative stress tolerance in bacteria." Biochem Soc Trans 33(Pt 1);176-80. PMID: 15667299

Poole94: Poole RK, Ioannidis N, Orii Y (1994). "Reactions of the Escherichia coli flavohaemoglobin (Hmp) with oxygen and reduced nicotinamide adenine dinucleotide: evidence for oxygen switching of flavin oxidoreduction and a mechanism for oxygen sensing." Proc R Soc Lond B Biol Sci 1994;255(1344);251-8. PMID: 8022841

Poole96: Poole RK, Ioannidis N, Orii Y (1996). "Reactions of the Escherichia coli flavohaemoglobin (Hmp) with NADH and near-micromolar oxygen: oxygen affinity of NADH oxidase activity." Microbiology 142 ( Pt 5);1141-8. PMID: 8704956

Poole96a: Poole RK, Anjum MF, Membrillo-Hernandez J, Kim SO, Hughes MN, Stewart V (1996). "Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12." J Bacteriol 178(18);5487-92. PMID: 8808940

Poole97: Poole RK, Rogers NJ, D'mello RA, Hughes MN, Orii Y (1997). "Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase activity to haem-bound dioxygen." Microbiology 143 ( Pt 5);1557-65. PMID: 9168606

Spiro06: Spiro S (2006). "Nitric oxide-sensing mechanisms in Escherichia coli." Biochem Soc Trans 34(Pt 1);200-2. PMID: 16417522

Stevanin00: Stevanin TM, Ioannidis N, Mills CE, Kim SO, Hughes MN, Poole RK (2000). "Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo' or bd, from nitric oxide." J Biol Chem 275(46);35868-75. PMID: 10915782

Stevanin07: Stevanin TM, Read RC, Poole RK (2007). "The hmp gene encoding the NO-inducible flavohaemoglobin in Escherichia coli confers a protective advantage in resisting killing within macrophages, but not in vitro: links with swarming motility." Gene 398(1-2);62-8. PMID: 17611046

Svensson06: Svensson L, Marklund BI, Poljakovic M, Persson K (2006). "Uropathogenic Escherichia coli and tolerance to nitric oxide: the role of flavohemoglobin." J Urol 175(2);749-53. PMID: 16407044

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Vasudevan91: Vasudevan SG, Armarego WL, Shaw DC, Lilley PE, Dixon NE, Poole RK (1991). "Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12." Mol Gen Genet 1991;226(1-2);49-58. PMID: 2034230

Vasudevan95: Vasudevan SG, Tang P, Dixon NE, Poole RK (1995). "Distribution of the flavohaemoglobin, HMP, between periplasm and cytoplasm in Escherichia coli." FEMS Microbiol Lett 1995;125(2-3);219-24. PMID: 7875569

Vine11a: Vine CE, Cole JA (2011). "Nitrosative stress in Escherichia coli: reduction of nitric oxide." Biochem Soc Trans 39(1);213-5. PMID: 21265775

Wu04a: Wu G, Corker H, Orii Y, Poole RK (2004). "Escherichia coli Hmp, an "oxygen-binding flavohaemoprotein", produces superoxide anion and self-destructs." Arch Microbiol 182(2-3);193-203. PMID: 15340787

Yohannes04: Yohannes E, Barnhart DM, Slonczewski JL (2004). "pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12." J Bacteriol 186(1);192-9. PMID: 14679238

Other References Related to Gene Regulation

Bodenmiller06: Bodenmiller DM, Spiro S (2006). "The yjeB (nsrR) gene of Escherichia coli encodes a nitric oxide-sensitive transcriptional regulator." J Bacteriol 188(3);874-81. PMID: 16428390

Crawford98: Crawford MJ, Goldberg DE (1998). "Regulation of the Salmonella typhimurium flavohemoglobin gene. A new pathway for bacterial gene expression in response to nitric oxide." J Biol Chem 273(51);34028-32. PMID: 9852058

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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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