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MetaCyc Polypeptide: cytochrome bo terminal oxidase subunit I

Gene: cyoB Accession Numbers: EG10179 (MetaCyc), b0431, ECK0425

Synonyms: cytochrome bo ubiquinol oxidase subunit I, cytochrome o ubiquinol oxidase subunit I

Species: Escherichia coli K-12 substr. MG1655

Component of: cytochrome bo terminal oxidase (extended summary available)

Summary:
cyoB encodes subunit I of the cytochrome bo terminal oxidase complex. The three prosthetic groups (heme O, heme B and CuB) are located in subunit 1 and are liganded by conserved histidine residues: His106 and His421 for heme B; His419 for heme O; His284, His333 and His334 for CuB ([Minagawa92, Lemieux92, Cheesman93, Calhoun93b, Calhoun93c, Calhoun93d, Tsubaki94, Uno94] and reviewed in [Tsubaki00]).The 3.5Å crystal structure confirmed these assignments [Abramson00]. Subunit 1 contains 15 transmembrane helices [Chepuri90]; helices 1-12 constitute a transmembrane barrel [Abramson00].

Mutation of a highly conserved amino acid (Asp135) in the cytochrome bo3 subunit I appears to decouple proton pumping from electron transfer-activity, which indicates that subunit I is likely to be involved in proton translocation [Thomas93]. Two polar cavities (the K and D channels), originating on the cytosolic side of the membrane and leading to the binuclear center are evident in the crystal structure and may function as proton transfer channels [Abramson00].

A potential ubiquinone binding site is located in the membrane domain of subunit I; it may represent the high affinity binding site (UQH); a low affinity binding site (UQL) could not be determined [Abramson00].

Mutation of the histidine residues that coordinate heme B and heme O result in defective assembly of the complex; mutation of residues coordinating the CuB center showed no effect on complex assembly [Stenberg07].

Citations: [Kobayashi09, Lin08, Thomas93a]

Locations: inner membrane

Map Position: [447,874 <- 449,865]

Molecular Weight of Polypeptide: 74.368 kD (from nucleotide sequence), 75.0 kD (experimental) [Nakamura97a ]

pI: 7.13

Unification Links: ASAP:ABE-0001493 , CGSC:30997 , DIP:DIP-47943N , DisProt:DP00088 , EchoBASE:EB0176 , EcoGene:EG10179 , EcoliWiki:b0431 , ModBase:P0ABI8 , OU-Microarray:b0431 , PortEco:cyoB , PR:PRO_000022369 , Pride:P0ABI8 , Protein Model Portal:P0ABI8 , RefSeq:NP_414965 , RegulonDB:EG10179 , SMR:P0ABI8 , String:511145.b0431 , UniProt:P0ABI8

Relationship Links: InterPro:IN-FAMILY:IPR000883 , InterPro:IN-FAMILY:IPR014207 , InterPro:IN-FAMILY:IPR023615 , InterPro:IN-FAMILY:IPR023616 , Panther:IN-FAMILY:PTHR10422 , PDB:Structure:1FFT , Pfam:IN-FAMILY:PF00115 , Prints:IN-FAMILY:PR01165 , Prosite:IN-FAMILY:PS00077 , Prosite:IN-FAMILY:PS50855

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment Inferred by computational analysis [GOA01a, Nakamura97a, Au85, Cotter90]
GO:0015990 - electron transport coupled proton transport Inferred from experiment [Richter93, Puustinen89]
GO:0019646 - aerobic electron transport chain Inferred from experiment [Matsushita86]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01a]
Molecular Function: GO:0005507 - copper ion binding Inferred from experiment [Minagawa92, Kita84, Abramson00]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14]
GO:0009055 - electron carrier activity Inferred from experiment Inferred by computational analysis [GOA01a, Matsushita84, Kita82, Puustinen91, Matsushita83]
GO:0009486 - cytochrome bo3 ubiquinol oxidase activity Inferred from experiment [Kita82, Matsushita83]
GO:0015078 - hydrogen ion transmembrane transporter activity Inferred from experiment [Thomas93, Puustinen91, Puustinen89]
GO:0015453 - oxidoreduction-driven active transmembrane transporter activity Inferred from experiment [Puustinen91, Puustinen89]
GO:0020037 - heme binding Inferred from experiment Inferred by computational analysis [GOA01a, Kita84, Abramson00, Minagawa92]
GO:0048039 - ubiquinone binding Inferred from experiment [Abramson00]
GO:0004129 - cytochrome-c oxidase activity Inferred by computational analysis [GOA01a]
GO:0005506 - iron ion binding Inferred by computational analysis [GOA01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
GO:0016682 - oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Nakamura90, DiazMejia09, Zhang07, Daley05]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis Inferred from experiment [Nakamura90, Saraste88, Abramson00]
GO:0009319 - cytochrome o ubiquinol oxidase complex Inferred from experiment [Abramson00, Matsushita83]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0070469 - respiratory chain Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon aerobic respiration
metabolism energy production/transport electron acceptors
transport Primary Active Transporters Oxidoreduction-driven Active Transporters

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Subunit of: cytochrome bo terminal oxidase

Synonyms: cytochrome bo3, cytochrome bo3 ubiquinol oxidase, cytochrome bo ubiquinol oxidase, cytochrome o ubiquinol oxidase

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of cytochrome bo terminal oxidase = [CyoD][CyoA][CyoB][CyoC]
         cytochrome bo terminal oxidase subunit IV = CyoD (summary available)
         cytochrome bo terminal oxidase subunit II = CyoA (extended summary available)
         cytochrome bo terminal oxidase subunit I = CyoB (extended summary available)
         cytochrome bo terminal oxidase subunit III = CyoC (summary available)

Summary:
The E. coli K-12 genome contains gene clusters for 3 cytochrome oxidase enzymes - cytochrome bo oxidase (CyoABCD), cytochrome bd-I oxidase (CydABX) and cytochrome bd-II oxidase (AppCD). The three enzymes function as the major terminal oxidases in the aerobic respiratory chain of E. coli. Cytochrome bo oxidase genes (cyoABCD) are expressed when oxygen levels are high while cytochrome bd-I oxidase genes are expressed under oxygen limited conditions [Tseng96]. Both enymes contribute to the generation of a proton motive force (PMF), cytochrome bo oxidase functions as a proton pump whilst cytochrome bd-I does not ([Puustinen91]). The energetics of cytochrome bd-II are less clear: initial reports suggested that it did not contribute to PMF [Bekker09] while later work suggested that it generated PMF with an H+/e- (protons translocated per electron) ratio of 0.94 [Borisov11].

The cytochrome bo terminal oxidase catalyzes the two-electron oxidation of ubiquinol within the membrane and the four-electron reduction of molecular oxygen to water. The enzyme contributes to the PMF [Kita82, Matsushita84, Matsushita86] (H+/e-=2) through its action as a proton pump (H+/e-=1) [Puustinen89] and through a redox loop mechanism (H+/e-=1) ([Puustinen91] and see review by [Unden97]).

Cytochrome bo terminal oxidase consists of four subunits (I - IV) encoded by the cyoB, cyoA, cyoC and cyoD genes respectively [Minghetti92], all of which are necessary for enzyme function [Nakamura97a]. The fifth gene of the cyo operon, cyoE encodes a heme O synthase which is essential for correct assembly of the complex [Hill92, Saiki93a]. Sequence analyses indicate that the complex is similar to the aa3-type family of cytochrome c oxidases [Saraste88, Chepuri90a]. The enzyme contains two heme groups - high spin heme O and low spin heme B - plus a single copper (CuB). The heme O and copper are magnetically coupled and constitute a heme-copper binuclear center which is the site of oxygen reduction. The enzyme lacks a CuA center which is typical of cytochrome c oxidases ([Salerno90, Puustinen91, Tsubaki93, Cheesman93] and reviewed by [Mogi94]).

The complex is thought to have 2 quinone binding sites - a low affinity QL site for ubiquinol oxidation and a high affinity QH site that mediates electron transfer from QL to heme B (the two step model for quinone binding) [SatoWatanabe94, Tsatsos98, SatoWatanabe94a, Yap10]

Analyses of intermediates in the assembly of cytochrome bo oxidase indicate that assembly of the complex is an ordered process whereby subunit III and IV assemble first, followed by subunit I and finally subunit II [Stenberg07].

A crystal structure of the entire cytochrome bo terminal oxidase complex has been determined at 3.5 Å resolution [Abramson00].

Expression of the cyo operon is negatively regulated by Fnr and the ArcA/ArcB two component system under anaerobic conditions [Iuchi90, Cotter90]. Expression varies depending on the carbon source used for growth - being highest on non-fermentable carbon sources and lowest on glucose [Cotter90]. Expression is induced by iron limitation [Cotter92].

Review: [GarciaHorsman94, Watmough98, Murray99]

Citations: [Szundi14, Morgan95, Svensson97, Mogi99, Welter94, Ma98, Weiss09, Ingledew93, Gohlke97, Abramson00a, Byrne00, Cheesman04, Oganesyan10, Butler97, Little96, Moody98, Moody97, Lin11, Musser97, Kobayashi00a, Lin12a, Grimaldi01, Hellwig02, Yap07, Yap06, SatoWatanabe95, Hellwig01, Hellwig99, Au87, Lorence87, Ma93a]

Locations: inner membrane

Relationship Links: PDB:Structure:1FFT

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [Nakamura97a, Au85, Cotter90]
GO:0015990 - electron transport coupled proton transport Inferred from experiment [Puustinen89]
GO:0019646 - aerobic electron transport chain Inferred from experiment [Matsushita86]
Molecular Function: GO:0005507 - copper ion binding Inferred from experiment [Kita84]
GO:0009055 - electron carrier activity Inferred from experiment [Matsushita83, Puustinen91, Kita82, Matsushita84]
GO:0009486 - cytochrome bo3 ubiquinol oxidase activity Inferred by computational analysis Inferred from experiment [Matsushita83, Kita82, GOA01a]
GO:0015078 - hydrogen ion transmembrane transporter activity Inferred from experiment [Puustinen91, Puustinen89]
GO:0015453 - oxidoreduction-driven active transmembrane transporter activity Inferred from experiment [Puustinen89, Puustinen91]
GO:0020037 - heme binding Inferred from experiment [Kita84]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment [Kita84]
GO:0005887 - integral component of plasma membrane Inferred from experiment Inferred by computational analysis [Saraste88, Abramson00]
GO:0009319 - cytochrome o ubiquinol oxidase complex Inferred from experiment [Minghetti92, Kita84]
GO:0016021 - integral component of membrane Inferred by computational analysis [GOA00]

Credits:
Revised in EcoCyc 17-Aug-2014 by Mackie A , Macquarie University
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: cytochrome bo terminal oxidase

Synonyms: cytochrome b562-o complex, cytochrome bo complex, cytochrome o complex, cytochrome o ubiquinol oxidase

EC Number: 1.10.3.10

In Pathways: succinate to cytochrome bo oxidase electron transfer , proline to cytochrome bo oxidase electron transfer , NADH to cytochrome bo oxidase electron transfer I , NADH to cytochrome bo oxidase electron transfer II , D-lactate to cytochrome bo oxidase electron transport , glycerol-3-phosphate to cytochrome bo oxidase electron transfer

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:

Citations: [Nakamura90, Puustinen89]

Cofactors or Prosthetic Groups: heme o [Minghetti92, Puustinen91], Cu2+ [Lemieux92, Minagawa92], ferroheme b [Kita84, Lemieux92, Minagawa92]

Activators (Unknown Mechanism): a phospholipid [Kita84]

Inhibitors (Noncompetitive): N,N-dimethylacetamide [Gupta08] , N,N-Dimethylformamide [Gupta08] , formamide [Gupta08]

Inhibitors (Unknown Mechanism): piericidin A [Kita86, Helmward89, Kita84] , potassium cyanide [Kita84] , hydroxylamine [Kita86, Helmward89] , 2-n-heptyl-4-hydroxyquinoline-N-oxide [Helmward89, Kita86, Kita84] , azide [Kita84] , Zn2+ [Helmward89, Kita86, Kita84] , Cd2+ [Kita84] , Co2+ [Kita84]


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 17 -> 35
[UniProt10]
UniProt: Helical; Name=I;
Transmembrane-Region 53 -> 80
[UniProt10]
UniProt: Helical; Name=II;
Mutagenesis-Variant 54
[Minagawa92, UniProt14]
Alternate sequence: A; UniProt: 50% quinol oxidase activity.
Mutagenesis-Variant 55
[Kawasaki97, UniProt11]
Alternate sequence: Q; UniProt: No effect.
Mutagenesis-Variant 71
[Hellwig02, Abramson00, UniProt14]
[Abramson00, UniProt11]
[Abramson00, UniProt11]
Alternate sequence: H; UniProt: No quinol oxidase activity.
Alternate sequence: L; UniProt: Abolishes enzyme activity.
Alternate sequence: Q; UniProt: Abolishes enzyme activity.
Amino-Acid-Sites-That-Bind 71
[UniProt14]
UniProt: Quinone (QH); Non-Experimental Qualifier: probable.
Mutagenesis-Variant 75
[Yap07, Hellwig02, Abramson00, UniProt14]
[Yap07, Hellwig02, Abramson00, UniProt14]
[Abramson00, UniProt11]
Alternate sequence: H; UniProt: No quinol oxidase activity, altered binding of a semiquinone intermediate at the QH site.
Alternate sequence: E; UniProt: Very similar to wild-type.
Alternate sequence: N; UniProt: Abolishes enzyme activity.
Amino-Acid-Sites-That-Bind 75
[UniProt14]
UniProt: Quinone (QH); Non-Experimental Qualifier: probable.
Mutagenesis-Variant 80
[Kawasaki97, UniProt11]
Alternate sequence: Q; UniProt: Abolishes enzyme activity.
Transmembrane-Region 96 -> 132
[UniProt10]
UniProt: Helical; Name=III;
Mutagenesis-Variant 98
[Hellwig02, Abramson00, UniProt14]
[Abramson00, UniProt11]
Alternate sequence: F; UniProt: About 1% quinol oxidase activity.
Alternate sequence: N; UniProt: Abolishes enzyme activity.
Amino-Acid-Sites-That-Bind 98
[UniProt14]
UniProt: Quinone (QH); Non-Experimental Qualifier: probable.
Amino-Acid-Sites-That-Bind 101
[UniProt14]
UniProt: Quinone (QH); Non-Experimental Qualifier: probable.
Mutagenesis-Variant 101
[Abramson00, UniProt11]
Alternate sequence: N; UniProt: Reduces enzyme activity by 75%.
Mutagenesis-Variant 102
[Hellwig02, UniProt14]
Alternate sequence: W; UniProt: No quinol oxidase activity.
Mutagenesis-Variant 106
[Minagawa92, UniProt14]
Alternate sequence: A; UniProt: 2% quinol oxidase activity, loss of heme b, loss of heme o, loss of Cu(B).
Metal-Binding-Site 106
[UniProt10a]
UniProt: Iron (heme B axial ligand); Non-Experimental Qualifier: probably;
Mutagenesis-Variant 135
[Kawasaki97, UniProt11]
Alternate sequence: N; UniProt: Abolishes enzyme activity.
Transmembrane-Region 138 -> 161
[UniProt10]
UniProt: Helical; Name=IV;
Mutagenesis-Variant 173
[Kawasaki97, UniProt11]
Alternate sequence: F; UniProt: No effect.
Transmembrane-Region 185 -> 215
[UniProt10]
UniProt: Helical; Name=V;
Mutagenesis-Variant 188
[Kawasaki97, UniProt11]
Alternate sequence: N; UniProt: No effect.
Transmembrane-Region 225 -> 260
[UniProt10]
UniProt: Helical; Name=VI;
Mutagenesis-Variant 256
[UniProt10]
Alternate sequence: N; UniProt: No effect;
Mutagenesis-Variant 257
[UniProt10]
Alternate sequence: Q; UniProt: Abolishes enzyme activity;
Transmembrane-Region 271 -> 307
[UniProt10]
UniProt: Helical; Name=VII;
Mutagenesis-Variant 284
[Minagawa92, UniProt14]
Alternate sequence: A; UniProt: 1% quinol oxidase activity, loss of heme o.
Crosslink-Site 288, 284
[UniProt10a]
UniProt: 1'-histidyl-3'-tyrosine (His-Tyr); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 284
[UniProt10a]
UniProt: Copper B; Non-Experimental Qualifier: probably;
Mutagenesis-Variant 286
[Kawasaki97, UniProt11]
Alternate sequence: D; UniProt: Great decrease in activity.
Alternate sequence: Q; UniProt: Great decrease in activity.
Mutagenesis-Variant 288
[Kawasaki97, UniProt11]
Alternate sequence: F; UniProt: Great decrease in activity.
Metal-Binding-Site 288
[UniProt10a]
UniProt: Copper B; Non-Experimental Qualifier: probably;
Transmembrane-Region 312 -> 326
[UniProt10]
UniProt: Helical; Name=VIII;
Mutagenesis-Variant 333
[Minagawa92, UniProt14]
Alternate sequence: A; UniProt: 2% quinol oxidase activity, loss of Cu(B).
Metal-Binding-Site 333
[UniProt10a]
UniProt: Copper B; Non-Experimental Qualifier: probably;
Mutagenesis-Variant 334
[Minagawa92, UniProt14]
Alternate sequence: A; UniProt: 1% quinol oxidase activity, loss of Cu(B).
Metal-Binding-Site 334
[UniProt10a]
UniProt: Copper B; Non-Experimental Qualifier: probably;
Transmembrane-Region 341 -> 369
[UniProt10]
UniProt: Helical; Name=IX;
Mutagenesis-Variant 362
[Kawasaki97, UniProt11]
Alternate sequence: Q; UniProt: Abolishes enzyme activity.
Transmembrane-Region 378 -> 409
[UniProt10]
UniProt: Helical; Name=X;
Mutagenesis-Variant 407
[Kawasaki97, UniProt11]
Alternate sequence: N; UniProt: Abolishes enzyme activity.
Mutagenesis-Variant 411
[Minagawa92, UniProt14]
Alternate sequence: A; UniProt: 50% quinol oxidase activity.
Transmembrane-Region 413 -> 445
[UniProt10]
UniProt: Helical; Name=XI;
Mutagenesis-Variant 419
[Minagawa92, UniProt14]
Alternate sequence: A; UniProt: 3% quinol oxidase activity, loss of heme o, loss of Cu(B).
Metal-Binding-Site 419
[UniProt10a]
UniProt: Iron (heme O axial ligand); Non-Experimental Qualifier: probably;
Mutagenesis-Variant 421
[Minagawa92, UniProt14]
Alternate sequence: A; UniProt: 1% quinol oxidase activity, loss of heme b, some loss of Cu(B).
Metal-Binding-Site 421
[UniProt10a]
UniProt: Iron (heme B axial ligand); Non-Experimental Qualifier: probably;
Transmembrane-Region 449 -> 477
[UniProt10]
UniProt: Helical; Name=XII;
Mutagenesis-Variant 481
[UniProt10]
Alternate sequence: Q; UniProt: No effect;
Mutagenesis-Variant 482
[UniProt10]
Alternate sequence: Q; UniProt: No effect;
Transmembrane-Region 490 -> 521
[UniProt10]
UniProt: Helical; Name=XIII;
Mutagenesis-Variant 540
[Kawasaki97, UniProt11]
Alternate sequence: Q; UniProt: Abolishes enzyme activity.
Transmembrane-Region 588 -> 606
[UniProt10]
UniProt: Helical; Name=XIV;
Transmembrane-Region 614 -> 632
[UniProt10]
UniProt: Helical; Name=XV;

History:
10/20/97 Gene b0431 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10179; confirmed by SwissProt match.


References

Abramson00: Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M (2000). "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol 7(10);910-7. PMID: 11017202

Abramson00a: Abramson J, Larsson G, Byrne B, Puustinen A, Garcia-Horsman A, Iwata S (2000). "Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coli." Acta Crystallogr D Biol Crystallogr 56(Pt 8);1076-8. PMID: 10944359

Au85: Au DC, Lorence RM, Gennis RB (1985). "Isolation and characterization of an Escherichia coli mutant lacking the cytochrome o terminal oxidase." J Bacteriol 161(1);123-7. PMID: 2981797

Au87: Au DC, Gennis RB (1987). "Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli." J Bacteriol 169(7);3237-42. PMID: 3036778

Bekker09: Bekker M, de Vries S, Ter Beek A, Hellingwerf KJ, de Mattos MJ (2009). "Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase." J Bacteriol 191(17);5510-7. PMID: 19542282

Borisov11: Borisov VB, Murali R, Verkhovskaya ML, Bloch DA, Han H, Gennis RB, Verkhovsky MI (2011). "Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode." Proc Natl Acad Sci U S A 108(42);17320-4. PMID: 21987791

Butler97: Butler CS, Seward HE, Greenwood C, Thomson AJ (1997). "Fast cytochrome bo from Escherichia coli binds two molecules of nitric oxide at CuB." Biochemistry 36(51);16259-66. PMID: 9405060

Byrne00: Byrne B, Abramson J, Jansson M, Holmgren E, Iwata S (2000). "Fusion protein approach to improve the crystal quality of cytochrome bo(3) ubiquinol oxidase from Escherichia coli." Biochim Biophys Acta 1459(2-3);449-55. PMID: 11004462

Calhoun93b: Calhoun MW, Hill JJ, Lemieux LJ, Ingledew WJ, Alben JO, Gennis RB (1993). "Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: amino acid substitutions for two histidines that are putative CuB ligands." Biochemistry 32(43);11524-9. PMID: 8218219

Calhoun93c: Calhoun MW, Thomas JW, Hill JJ, Hosler JP, Shapleigh JP, Tecklenburg MM, Ferguson-Miller S, Babcock GT, Alben JO, Gennis RB (1993). "Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides." Biochemistry 32(40);10905-11. PMID: 8399240

Calhoun93d: Calhoun MW, Lemieux LJ, Thomas JW, Hill JJ, Goswitz VC, Alben JO, Gennis RB (1993). "Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli." Biochemistry 32(48);13254-61. PMID: 8241181

Cheesman04: Cheesman MR, Oganesyan VS, Watmough NJ, Butler CS, Thomson AJ (2004). "The nature of the exchange coupling between high-spin Fe(III) heme o3 and CuBII in Escherichia coli quinol oxidase, cytochrome bo3: MCD and EPR studies." J Am Chem Soc 126(13);4157-66. PMID: 15053605

Cheesman93: Cheesman MR, Watmough NJ, Pires CA, Turner R, Brittain T, Gennis RB, Greenwood C, Thomson AJ (1993). "Cytochrome bo from Escherichia coli: identification of haem ligands and reaction of the reduced enzyme with carbon monoxide." Biochem J 289 ( Pt 3);709-18. PMID: 8382047

Chepuri90: Chepuri V, Gennis RB (1990). "The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli." J Biol Chem 265(22);12978-86. PMID: 2165491

Chepuri90a: Chepuri V, Lemieux L, Au DC, Gennis RB (1990). "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem 265(19);11185-92. PMID: 2162835

Cotter90: Cotter PA, Chepuri V, Gennis RB, Gunsalus RP (1990). "Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product." J Bacteriol 172(11);6333-8. PMID: 2172211

Cotter92: Cotter PA, Darie S, Gunsalus RP (1992). "The effect of iron limitation on expression of the aerobic and anaerobic electron transport pathway genes in Escherichia coli." FEMS Microbiol Lett 79(1-3);227-32. PMID: 1478458

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

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

GarciaHorsman94: Garcia-Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB (1994). "The superfamily of heme-copper respiratory oxidases." J Bacteriol 176(18);5587-600. PMID: 8083153

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

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

Gohlke97: Gohlke U, Warne A, Saraste M (1997). "Projection structure of the cytochrome bo ubiquinol oxidase from Escherichia coli at 6 A resolution." EMBO J 16(6);1181-8. PMID: 9135135

Grimaldi01: Grimaldi S, MacMillan F, Ostermann T, Ludwig B, Michel H, Prisner T (2001). "QH*- ubisemiquinone radical in the bo3-type ubiquinol oxidase studied by pulsed electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy." Biochemistry 40(4);1037-43. PMID: 11170426

Gupta08: Gupta S, Mazumdar S (2008). "Inhibition of bacterial oxidases by formamide and analogues." Biol Chem 389(5):599-607. PMID: 18321216

Hellwig01: Hellwig P, Barquera B, Gennis RB (2001). "Direct evidence for the protonation of aspartate-75, proposed to be at a quinol binding site, upon reduction of cytochrome bo3 from Escherichia coli." Biochemistry 40(4);1077-82. PMID: 11170431

Hellwig02: Hellwig P, Yano T, Ohnishi T, Gennis RB (2002). "Identification of the residues involved in stabilization of the semiquinone radical in the high-affinity ubiquinone binding site in cytochrome bo(3) from Escherichia coli by site-directed mutagenesis and EPR spectroscopy." Biochemistry 41(34);10675-9. PMID: 12186553

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