메뉴 건너뛰기




Volumn 43, Issue 8, 2004, Pages 2217-2227

The Raised Midpoint Potential of the [2Fe2S] Cluster of Cytochrome bc 1 Is Mediated by Both the Qo Site Occupants and the Head Domain Position of the Fe-S Protein Subunit

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CATALYSIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYMES; HYDROGEN BONDS; MICROORGANISMS;

EID: 1442325507     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035938u     Document Type: Article
Times cited : (35)

References (41)
  • 11
    • 0034624079 scopus 로고    scopus 로고
    • 1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein
    • 1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein. J. Biol. Chem. 275, 38597-38604.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38597-38604
    • Xiao, K.H.1    Yu, L.2    Yu, C.A.3
  • 25
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton, P. L. (1978) Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol. 54, 411-435
    • (1978) Methods Enzymol. , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 26
    • 0021830124 scopus 로고
    • The Chromone inhibitor stigmatellin binding to the ubiquinol oxidation center at the c-side of the mitochondrial-membrane
    • von Jagow, G., and Ohnishi, T. (1985) The Chromone inhibitor stigmatellin binding to the ubiquinol oxidation center at the c-side of the mitochondrial-membrane. FEBS Lett. 185, 311-315.
    • (1985) FEBS Lett. , vol.185 , pp. 311-315
    • Von Jagow, G.1    Ohnishi, T.2
  • 27
    • 0020567816 scopus 로고
    • Inhibition of electron-transfer by 3-alkyl-2-hydroxy-1,4-naphthoquinones in the ubiquinol-cytochrome-c oxidoreductases of Rhodopseudomonas-sphaeroides and mammalian mitochondria - Interaction with a ubiquinone-binding site and the Rieske iron-sulfur cluster
    • Matsuura, K., Bowyer, J. R., Ohnishi, T., and Dutton, P. L. (1983) Inhibition of electron-transfer by 3-alkyl-2-hydroxy-1,4-naphthoquinones in the ubiquinol-cytochrome-c oxidoreductases of Rhodopseudomonas-sphaeroides and mammalian mitochondria - Interaction with a ubiquinone-binding site and the Rieske iron-sulfur cluster. J. Biol. Chem. 258, 1571-1579.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1571-1579
    • Matsuura, K.1    Bowyer, J.R.2    Ohnishi, T.3    Dutton, P.L.4
  • 31
    • 0019883397 scopus 로고
    • The recognition and redox properties of a component, possibly a quinone, which determines electron-transfer rate in ubiquinone-cytochrome-c oxidoreductase of mitochondria
    • Matsuura, K., Packham, N. K., Mueller, P., and Dutton, P. L. (1981) The recognition and redox properties of a component, possibly a quinone, which determines electron-transfer rate in ubiquinone-cytochrome-c oxidoreductase of mitochondria. FEBS Lett. 131, 17-22.
    • (1981) FEBS Lett. , vol.131 , pp. 17-22
    • Matsuura, K.1    Packham, N.K.2    Mueller, P.3    Dutton, P.L.4
  • 34
    • 0032587408 scopus 로고    scopus 로고
    • o site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton
    • o site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton. FEBS Lett. 450, 245-250.
    • (1999) FEBS Lett. , vol.450 , pp. 245-250
    • Schoepp, B.1    Brugna, M.2    Riedel, A.3    Nitschke, W.4    Kramer, D.M.5
  • 35
    • 0039207658 scopus 로고
    • The location, orientation and stiochiometry of the Rieske iron-sulfur cluster in membranes from Rhodopseudomonas sphaeroides
    • Prince, R. C. (1983) The location, orientation and stiochiometry of the Rieske iron-sulfur cluster in membranes from Rhodopseudomonas sphaeroides. Biochim. Biophys. Acta 723, 133-138.
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 133-138
    • Prince, R.C.1
  • 39
    • 0037433194 scopus 로고    scopus 로고
    • Correlation between hydrogen bond lengths and reduction potentials in Clostridium pasteurianum rubredoxin
    • Lin, I. J., Gebel, E. B., Machonkin, T. E., Westler, W. M., and Markley, J. L. (2003) Correlation between hydrogen bond lengths and reduction potentials in Clostridium pasteurianum rubredoxin. J. Am. Chem. Soc. 125, 1464-1465.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1464-1465
    • Lin, I.J.1    Gebel, E.B.2    Machonkin, T.E.3    Westler, W.M.4    Markley, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.