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MetaCyc Polypeptide: cytochrome bo terminal oxidase subunit III

Gene: cyoC Accession Numbers: EG10180 (MetaCyc), b0430, ECK0424

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

Species: Escherichia coli K-12 substr. MG1655

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

Summary:
CyoC is subunit III of the 4 subunit cytochrome bo terminal oxidase complex in E. coli K-12. Subunit III is required for expression of a functional complex [Nakamura97]

The CyoC polypeptide contains five transmembrane helices [Chepuri90, Abramson00].

Locations: inner membrane

Map Position: [447,270 <- 447,884]

Molecular Weight of Polypeptide: 22.623 kD (from nucleotide sequence), 20.5 kD (experimental) [Nakamura97 ]

pI: 7.03

Unification Links: ASAP:ABE-0001491 , CGSC:31005 , DIP:DIP-47944N , EchoBASE:EB0177 , EcoGene:EG10180 , EcoliWiki:b0430 , ModBase:P0ABJ3 , OU-Microarray:b0430 , PortEco:cyoC , PR:PRO_000022370 , Protein Model Portal:P0ABJ3 , RefSeq:NP_414964 , RegulonDB:EG10180 , SMR:P0ABJ3 , String:511145.b0430 , UniProt:P0ABJ3

Relationship Links: InterPro:IN-FAMILY:IPR000298 , InterPro:IN-FAMILY:IPR013833 , InterPro:IN-FAMILY:IPR014206 , InterPro:IN-FAMILY:IPR024791 , Panther:IN-FAMILY:PTHR11403 , PDB:Structure:1FFT , Pfam:IN-FAMILY:PF00510 , Prosite:IN-FAMILY:PS50253

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [Nakamura97, Au85, Cotter90]
GO:0015990 - electron transport coupled proton transport Inferred from experiment [Puustinen89]
GO:0019646 - aerobic electron transport chain Inferred from experiment Inferred by computational analysis [GOA01, Matsushita86]
GO:0022904 - respiratory electron transport chain Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Abramson00]
GO:0009055 - electron carrier activity Inferred from experiment [Matsushita84, Kita82, Puustinen91, Matsushita83]
GO:0009486 - cytochrome bo3 ubiquinol oxidase activity Inferred by computational analysis Inferred from experiment [Kita82, Matsushita83, GOA01]
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:0004129 - cytochrome-c oxidase activity Inferred by computational analysis [GOA01]
GO:0008827 - cytochrome o ubiquinol oxidase activity Inferred by computational analysis [GOA01]
GO:0015002 - heme-copper terminal oxidase activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA01, DiazMejia09, Zhang07, Daley05]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Abramson00]
GO:0009319 - cytochrome o ubiquinol oxidase complex Inferred from experiment [Nakamura97, Abramson00]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane 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:
Reviewed in EcoCyc 06-Apr-2008 by Nolan L , Macquarie University
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 [Nakamura97]. The fifth gene of the cyo operon, cyoE encodes a heme O synthase which is essential for correct assembly of the complex [Hill92, Saiki93]. 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 [Iuchi90b, 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, Murray99a]

Citations: [Szundi14, Morgan95, Svensson97, Mogi99, Welter94, Ma98, Weiss09, Ingledew93, Gohlke97, Abramson00a, Byrne00, Cheesman04, Oganesyan10, Butler97, Little96, Moody98, Moody97, Lin11b, Musser97, Kobayashi00a, Lin12b, 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 [Nakamura97, 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, GOA01]
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 32 -> 50
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probably;
Transmembrane-Region 67 -> 85
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probably;
Transmembrane-Region 102 -> 120
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probably;
Transmembrane-Region 143 -> 161
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probably;
Transmembrane-Region 185 -> 203
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probably;

History:
10/20/97 Gene b0430 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10180; 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

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."

GOA01: 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

Hellwig99: Hellwig P, Mogi T, Tomson FL, Gennis RB, Iwata J, Miyoshi H, Mantele W (1999). "Vibrational modes of ubiquinone in cytochrome bo(3) from Escherichia coli identified by Fourier transform infrared difference spectroscopy and specific (13)C labeling." Biochemistry 38(44);14683-9. PMID: 10545194

Helmward89: Helmward Z "Handbook of Enzyme Inhibitors. 2nd, revised and enlarged edition." Weinheim, Federal Republic of Germany ; New York, NY, USA , 1989.

Hill92: Hill J, Goswitz VC, Calhoun M, Garcia-Horsman JA, Lemieux L, Alben JO, Gennis RB (1992). "Demonstration by FTIR that the bo-type ubiquinol oxidase of Escherichia coli contains a heme-copper binuclear center similar to that in cytochrome c oxidase and that proper assembly of the binuclear center requires the cyoE gene product." Biochemistry 31(46);11435-40. PMID: 1332759

Ingledew93: Ingledew WJ, Horrocks J, Salerno JC (1993). "Ligand binding to the haem-copper binuclear catalytic site of cytochrome bo, a respiratory quinol oxidase from Escherichia coli." Eur J Biochem 212(3);657-64. PMID: 8385006

Iuchi90b: Iuchi S, Chepuri V, Fu HA, Gennis RB, Lin EC (1990). "Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: study utilizing deletions and lac fusions of cyo and cyd." J Bacteriol 172(10);6020-5. PMID: 2170337

Kita82: Kita K, Kasahara M, Anraku Y (1982). "Formation of a membrane potential by reconstructed liposomes made with cytochrome b562-o complex, a terminal oxidase of Escherichia coli K12." J Biol Chem 257(14);7933-5. PMID: 7045115

Kita84: Kita K, Konishi K, Anraku Y (1984). "Terminal oxidases of Escherichia coli aerobic respiratory chain. I. Purification and properties of cytochrome b562-o complex from cells in the early exponential phase of aerobic growth." J Biol Chem 1984;259(5);3368-74. PMID: 6365921

Kita86: Kita K, Konishi K, Anraku Y (1986). "Purification and properties of two terminal oxidase complexes of Escherichia coli aerobic respiratory chain." Methods Enzymol 1986;126;94-113. PMID: 2856144

Kobayashi00a: Kobayashi K, Tagawa S, Mogi T (2000). "Transient formation of ubisemiquinone radical and subsequent electron transfer process in the Escherichia coli cytochrome bo." Biochemistry 39(50);15620-5. PMID: 11112550

Lemieux92: Lemieux LJ, Calhoun MW, Thomas JW, Ingledew WJ, Gennis RB (1992). "Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis." J Biol Chem 1992;267(3);2105-13. PMID: 1309809

Lin11b: Lin MT, Shubin AA, Samoilova RI, Narasimhulu KV, Baldansuren A, Gennis RB, Dikanov SA (2011). "Exploring by pulsed EPR the electronic structure of ubisemiquinone bound at the QH site of cytochrome bo3 from Escherichia coli with in vivo 13C-labeled methyl and methoxy substituents." J Biol Chem 286(12);10105-14. PMID: 21247900

Lin12b: Lin MT, Baldansuren A, Hart R, Samoilova RI, Narasimhulu KV, Yap LL, Choi SK, O'Malley PJ, Gennis RB, Dikanov SA (2012). "Interactions of intermediate semiquinone with surrounding protein residues at the Q(H) site of wild-type and D75H mutant cytochrome bo3 from Escherichia coli." Biochemistry 51(18);3827-38. PMID: 22497216

Little96: Little RH, Cheesman MR, Thomson AJ, Greenwood C, Watmough NJ (1996). "Cytochrome bo from Escherichia coli: binding of azide to CuB." Biochemistry 35(43);13780-7. PMID: 8901520

Lorence87: Lorence RM, Carter K, Green GN, Gennis RB (1987). "Cytochrome b558 monitors the steady state redox state of the ubiquinone pool in the aerobic respiratory chain of Escherichia coli." J Biol Chem 262(22);10532-6. PMID: 3301837

Ma93a: Ma J, Lemieux L, Gennis RB (1993). "Genetic fusion of subunits I, II, and III of the cytochrome bo ubiquinol oxidase from Escherichia coli results in a fully assembled and active enzyme." Biochemistry 32(30);7692-7. PMID: 8394111

Ma98: Ma J, Puustinen A, Wikstrom M, Gennis RB (1998). "Tryptophan-136 in subunit II of cytochrome bo3 from Escherichia coli may participate in the binding of ubiquinol." Biochemistry 37(34);11806-11. PMID: 9718303

Matsushita83: Matsushita K, Patel L, Gennis RB, Kaback HR (1983). "Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from Escherichia coli." Proc Natl Acad Sci U S A 80(16);4889-93. PMID: 6308657

Matsushita84: Matsushita K, Patel L, Kaback HR (1984). "Cytochrome o type oxidase from Escherichia coli. Characterization of the enzyme and mechanism of electrochemical proton gradient generation." Biochemistry 23(20);4703-14. PMID: 6093862

Matsushita86: Matsushita K, Kaback HR (1986). "D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase." Biochemistry 25(9);2321-7. PMID: 3013300

Minagawa92: Minagawa J, Mogi T, Gennis RB, Anraku Y (1992). "Identification of heme and copper ligands in subunit I of the cytochrome bo complex in Escherichia coli." J Biol Chem 1992;267(3);2096-104. PMID: 1309808

Minghetti92: Minghetti KC, Goswitz VC, Gabriel NE, Hill JJ, Barassi CA, Georgiou CD, Chan SI, Gennis RB (1992). "Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity." Biochemistry 31(30);6917-24. PMID: 1322173

Mogi94: Mogi T, Nakamura H, Anraku Y (1994). "Molecular structure of a heme-copper redox center of the Escherichia coli ubiquinol oxidase: evidence and model." J Biochem 116(3);471-7. PMID: 7852262

Mogi99: Mogi T, Sato-Watanabe M, Miyoshi H, Orii Y (1999). "Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygen." FEBS Lett 457(2);223-6. PMID: 10471783

Moody97: Moody AJ, Mitchell R, Jeal AE, Rich PR (1997). "Comparison of the ligand-binding properties of native and copper-less cytochromes bo from Escherichia coli." Biochem J 324 ( Pt 3);743-52. PMID: 9210397

Moody98: Moody AJ, Butler CS, Watmough NJ, Thomson AJ, Rich PR (1998). "The reaction of halides with pulsed cytochrome bo from Escherichia coli." Biochem J 331 ( Pt 2);459-64. PMID: 9531485

Morgan95: Morgan JE, Verkhovsky MI, Puustinen A, Wikstrom M (1995). "Identification of a "peroxy" intermediate in cytochrome bo3 of Escherichia coli." Biochemistry 34(48);15633-7. PMID: 7495791

Murray99a: Murray L, Pires RH, Hastings SF, Ingledew WJ (1999). "Models for structure and function in quinone-binding sites: the Escherichia coli quinol oxidase, cytochrome bo3." Biochem Soc Trans 27(4);581-5. PMID: 10917646

Musser97: Musser SM, Stowell MH, Lee HK, Rumbley JN, Chan SI (1997). "Uncompetitive substrate inhibition and noncompetitive inhibition by 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole (UHDBT) and 2-n-nonyl-4-hydroxyquinoline-N-oxide (NQNO) is observed for the cytochrome bo3 complex: implications for a Q(H2)-loop proton translocation mechanism." Biochemistry 36(4);894-902. PMID: 9020789

Nakamura90: Nakamura H, Yamato I, Anraku Y, Lemieux L, Gennis RB (1990). "Expression of cyoA and cyoB demonstrates that the CO-binding heme component of the Escherichia coli cytochrome o complex is in subunit I." J Biol Chem 1990;265(19);11193-7. PMID: 2162836

Nakamura97: Nakamura H, Saiki K, Mogi T, Anraku Y (1997). "Assignment and functional roles of the cyoABCDE gene products required for the Escherichia coli bo-type quinol oxidase." J Biochem 122(2);415-21. PMID: 9378722

Oganesyan10: Oganesyan VS, White GF, Field S, Marritt S, Gennis RB, Yap LL, Thomson AJ (2010). "Nitroxide spin labels as EPR reporters of the relaxation and magnetic properties of the heme-copper site in cytochrome bo3, E. coli." J Biol Inorg Chem 15(8);1255-64. PMID: 20623242

Puustinen89: Puustinen A, Finel M, Virkki M, Wikstrom M (1989). "Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli." FEBS Lett 249(2);163-7. PMID: 2544445

Puustinen91: Puustinen A, Finel M, Haltia T, Gennis RB, Wikstrom M (1991). "Properties of the two terminal oxidases of Escherichia coli." Biochemistry 30(16);3936-42. PMID: 1850294

Saiki93: Saiki K, Mogi T, Ogura K, Anraku Y (1993). "In vitro heme O synthesis by the cyoE gene product from Escherichia coli." J Biol Chem 1993;268(35);26041-4. PMID: 8253713

Salerno90: Salerno JC, Bolgiano B, Poole RK, Gennis RB, Ingledew WJ (1990). "Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli." J Biol Chem 265(8);4364-8. PMID: 2155226

Saraste88: Saraste M, Raitio M, Jalli T, Chepuri V, Lemieux L, Gennis RB (1988). "Cytochrome o from Escherichia coli is structurally related to cytochrome aa3." Ann N Y Acad Sci 550;314-24. PMID: 2854403

SatoWatanabe94: Sato-Watanabe M, Mogi T, Ogura T, Kitagawa T, Miyoshi H, Iwamura H, Anraku Y (1994). "Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli." J Biol Chem 269(46);28908-12. PMID: 7961852

SatoWatanabe94a: Sato-Watanabe M, Mogi T, Miyoshi H, Iwamura H, Matsushita K, Adachi O, Anraku Y (1994). "Structure-function studies on the ubiquinol oxidation site of the cytochrome bo complex from Escherichia coli using p-benzoquinones and substituted phenols." J Biol Chem 269(46);28899-907. PMID: 7961851

SatoWatanabe95: Sato-Watanabe M, Itoh S, Mogi T, Matsuura K, Miyoshi H, Anraku Y (1995). "Stabilization of a semiquinone radical at the high-affinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase." FEBS Lett 374(2);265-9. PMID: 7589550

Stenberg07: Stenberg F, von Heijne G, Daley DO (2007). "Assembly of the cytochrome bo3 complex." J Mol Biol 371(3);765-73. PMID: 17583738

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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