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Volumn 1658, Issue 1-2, 2004, Pages 165-171

The quinone chemistry of bc complexes

Author keywords

Cytochrome bc complex; Em; Electrochemistry; ISP; Q cycle; Rieske iron sulfur protein; SHE; standard hydrogen electrode; Subscripts ox and red; the oxidized and reduced states; Ubiquinone

Indexed keywords

1,4 BENZOQUINONE; HYDROGEN; PROTON; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 3542991515     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.04.021     Document Type: Review
Times cited : (89)

References (41)
  • 8
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P. Possible molecular mechanisms of the protonmotive function of cytochrome systems. J. Theor. Biol. 62:1976;327-367
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 9
    • 0030001519 scopus 로고    scopus 로고
    • 1 complex by proton-gated charge-transfer
    • 1 complex by proton-gated charge-transfer. FEBS Lett. 387:1996;1-6
    • (1996) FEBS Lett. , vol.387 , pp. 1-6
    • Brandt, U.1
  • 15
    • 0030861648 scopus 로고    scopus 로고
    • 1 complex
    • 1 complex. FEBS Lett. 412:1997;257-264
    • (1997) FEBS Lett. , vol.412 , pp. 257-264
    • Link, T.A.1
  • 16
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • Trumpower B.L., Gennis R.B. Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation. Annu. Rev. Biochem. 63:1994;675-716
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 18
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • Osyczka A., Moser C.C., Daldal F., Dutton P.L. Reversible redox energy coupling in electron transfer chains. Nature. 427:2004;607-612
    • (2004) Nature , vol.427 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daldal, F.3    Dutton, P.L.4
  • 19
    • 0019316012 scopus 로고
    • The kinetics and thermodynamics of the reduction of cytochrome c by substituted p-benzoquinols in solution
    • Rich P.R., Bendall D.S. The kinetics and thermodynamics of the reduction of cytochrome c by substituted p-benzoquinols in solution. Biochim. Biophys. Acta. 592:1980;506-518
    • (1980) Biochim. Biophys. Acta , vol.592 , pp. 506-518
    • Rich, P.R.1    Bendall, D.S.2
  • 20
    • 0021758697 scopus 로고
    • Electron and proton transfers through quinones and cytochrome bc complexes
    • Rich P.R. Electron and proton transfers through quinones and cytochrome bc complexes. Biochim. Biophys. Acta. 768:1984;53-79
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 53-79
    • Rich, P.R.1
  • 21
    • 0020353465 scopus 로고
    • Electron and proton transfers in chemical and biological quinone systems
    • Rich P.R. Electron and proton transfers in chemical and biological quinone systems. Faraday Discuss. Chem. Soc. 74:1982;349-364
    • (1982) Faraday Discuss. Chem. Soc. , vol.74 , pp. 349-364
    • Rich, P.R.1
  • 22
    • 0003159212 scopus 로고
    • Electron transfer reactions between quinols and quinones in aqueous and aprotic media
    • Rich P.R. Electron transfer reactions between quinols and quinones in aqueous and aprotic media. Biochim. Biophys. Acta. 637:1981;28-33
    • (1981) Biochim. Biophys. Acta , vol.637 , pp. 28-33
    • Rich, P.R.1
  • 25
    • 0024276081 scopus 로고
    • Characterisation of binding of the methoxyacrylate inhibitors to mitochondrial cytochrome c reductase
    • Brandt U., Schägger H., von Jagow G. Characterisation of binding of the methoxyacrylate inhibitors to mitochondrial cytochrome c reductase. Eur. J. Biochem. 173:1988;499-506
    • (1988) Eur. J. Biochem. , vol.173 , pp. 499-506
    • Brandt, U.1    Schägger, H.2    Von Jagow, G.3
  • 27
    • 0015909789 scopus 로고
    • Further evidence for the pool function of ubiquinone as derived from the inhibition of the electron transport by antimycin
    • Kröger A., Klingenberg M. Further evidence for the pool function of ubiquinone as derived from the inhibition of the electron transport by antimycin. Eur. J. Biochem. 39:1973;313-323
    • (1973) Eur. J. Biochem. , vol.39 , pp. 313-323
    • Kröger, A.1    Klingenberg, M.2
  • 32
    • 0037059734 scopus 로고    scopus 로고
    • 1 complex. Evidence for an alternating, half-of-the-sites mechanism of ubiquinol oxidation
    • 1 complex. Evidence for an alternating, half-of-the-sites mechanism of ubiquinol oxidation. J. Biol. Chem. 277:2002;1195-1202
    • (2002) J. Biol. Chem. , vol.277 , pp. 1195-1202
    • Gutierrez-Cirlos, E.B.1    Trumpower, B.L.2
  • 35
    • 3543039192 scopus 로고    scopus 로고
    • 1 complex: Tentative reaction mechanism and prevention of short-circuiting
    • (in press)
    • 1 complex: tentative reaction mechanism and prevention of short-circuiting. Biochim. Biophys. Acta. 2004;. (in press)
    • (2004) Biochim. Biophys. Acta
    • Mulkidjanian, A.1
  • 36
    • 33750639677 scopus 로고
    • The key-lock theory and the induced fit theory
    • Koshland D.E. Jr. The key-lock theory and the induced fit theory. Angew. Chem., Int. Ed. Engl. 33:1994;2375-2378
    • (1994) Angew. Chem., Int. Ed. Engl. , vol.33 , pp. 2375-2378
    • Koshland Jr., D.E.1
  • 37
    • 0028220770 scopus 로고
    • Two pK values of the oxidised 'Rieske' [2Fe-2S] cluster observed by CD spectroscopy
    • Link T.A. Two pK values of the oxidised 'Rieske' [2Fe-2S] cluster observed by CD spectroscopy. Biochim. Biophys. Acta. 1185:1994;81-84
    • (1994) Biochim. Biophys. Acta , vol.1185 , pp. 81-84
    • Link, T.A.1
  • 38
    • 0035840956 scopus 로고    scopus 로고
    • 1-type Rieske [2Fe-2S] center of Thermus thermophilus
    • 1-type Rieske [2Fe-2S] center of Thermus thermophilus. J. Amer. Chem. Soc. 123:2001;9906-9907
    • (2001) J. Amer. Chem. Soc. , vol.123 , pp. 9906-9907
    • Zu, Y.1    Fee, J.A.2    Hirst, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.