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Journal Abstract Search

186 related items for PubMed ID: 10471783

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  • 3. Transient formation of ubisemiquinone radical and subsequent electron transfer process in the Escherichia coli cytochrome bo.
    Kobayashi K, Tagawa S, Mogi T.
    Biochemistry; 2000 Dec 19; 39(50):15620-5. PubMed ID: 11112550
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  • 8. Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule.
    Puustinen A, Verkhovsky MI, Morgan JE, Belevich NP, Wikstrom M.
    Proc Natl Acad Sci U S A; 1996 Feb 20; 93(4):1545-8. PubMed ID: 8643669
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  • 12. Reaction of Escherichia coli cytochrome bo3 with substoichiometric ubiquinol-2: a freeze-quench electron paramagnetic resonance investigation.
    Schultz BE, Edmondson DE, Chan SI.
    Biochemistry; 1998 Mar 24; 37(12):4160-8. PubMed ID: 9521737
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  • 15. Structure-function studies on the ubiquinol oxidation site of the cytochrome bo complex from Escherichia coli using p-benzoquinones and substituted phenols.
    Sato-Watanabe M, Mogi T, Miyoshi H, Iwamura H, Matsushita K, Adachi O, Anraku Y.
    J Biol Chem; 1994 Nov 18; 269(46):28899-907. PubMed ID: 7961851
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  • 16. 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.
    Musser SM, Stowell MH, Lee HK, Rumbley JN, Chan SI.
    Biochemistry; 1997 Jan 28; 36(4):894-902. PubMed ID: 9020789
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  • 17. Characterization of the ubiquinol oxidation sites in cytochromes bo and bd from Escherichia coli using aurachin C analogues.
    Miyoshi H, Takegami K, Sakamoto K, Mogi T, Iwamura H.
    J Biochem; 1999 Jan 28; 125(1):138-42. PubMed ID: 9880809
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  • 18. Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli.
    Sato-Watanabe M, Mogi T, Ogura T, Kitagawa T, Miyoshi H, Iwamura H, Anraku Y.
    J Biol Chem; 1994 Nov 18; 269(46):28908-12. PubMed ID: 7961852
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