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129 related items for PubMed ID: 8025668

  • 1. The high-spin cytochrome o' component of the cytochrome bo-type quinol oxidase in membranes from Escherichia coli: formation of the primary oxygenated species at low temperatures is characterized by a slow 'on' rate and low dissociation constant.
    Poole RK, Salmon I, Chance B.
    Microbiology (Reading); 1994 May; 140 ( Pt 5)():1027-34. PubMed ID: 8025668
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  • 3. The reaction of cytochrome o in Escherichia coli K12 with oxygen. Evidence for a spectrally and kinetically distinct cytochrome o in cells from oxygen-limited cultures.
    Poole RK, Chance B.
    J Gen Microbiol; 1981 Oct; 126(2):277-87. PubMed ID: 7040597
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  • 5. The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli.
    Hill BC, Hill JJ, Gennis RB.
    Biochemistry; 1994 Dec 20; 33(50):15110-5. PubMed ID: 7999770
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  • 6. Cytochrome bo from Escherichia coli: identification of haem ligands and reaction of the reduced enzyme with carbon monoxide.
    Cheesman MR, Watmough NJ, Pires CA, Turner R, Brittain T, Gennis RB, Greenwood C, Thomson AJ.
    Biochem J; 1993 Feb 01; 289 ( Pt 3)(Pt 3):709-18. PubMed ID: 8382047
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  • 9. The reaction of cytochrome omicron in Escherichia coli with oxygen. Low-temperature kinetic and spectral studies.
    Poole RK, Waring AJ, Chance B.
    Biochem J; 1979 Nov 15; 184(2):379-89. PubMed ID: 393255
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  • 16. Cytochrome bo from Escherichia coli: reaction of the oxidized enzyme with hydrogen peroxide.
    Watmough NJ, Cheesman MR, Greenwood C, Thomson AJ.
    Biochem J; 1994 Jun 01; 300 ( Pt 2)(Pt 2):469-75. PubMed ID: 8002953
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  • 17. Photodissociation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation.
    Orii Y, Webster DA.
    J Biol Chem; 1986 Mar 15; 261(8):3544-7. PubMed ID: 3949777
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  • 18. Effects of replacement of low-spin haem b by haem O on Escherichia coli cytochromes bo and bd quinol oxidases.
    Mogi T.
    J Biochem; 2009 May 15; 145(5):599-607. PubMed ID: 19174546
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  • 19. Flash photolysis of the carbon monoxide compounds of wild-type and mutant variants of cytochrome bo from Escherichia coli.
    Brown S, Rumbley JN, Moody AJ, Thomas JW, Gennis RB, Rich PR.
    Biochim Biophys Acta; 1994 Jan 04; 1183(3):521-32. PubMed ID: 8286401
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  • 20. Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli.
    Salerno JC, Bolgiano B, Poole RK, Gennis RB, Ingledew WJ.
    J Biol Chem; 1990 Mar 15; 265(8):4364-8. PubMed ID: 2155226
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