메뉴 건너뛰기




Volumn 47, Issue 47, 2008, Pages 12365-12370

Movement of the iron-sulfur head domain of cytochrome bc1 transiently opens the catalytic Qo site for reaction with oxygen

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON GUNS; ELECTRONS; ENERGY CONVERSION; ENZYMES; HEMOGLOBIN; LEAKAGE (FLUID); NETWORKS (CIRCUITS); PORPHYRINS; PROBABILITY; SULFUR;

EID: 56749172576     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801207f     Document Type: Article
Times cited : (53)

References (34)
  • 2
    • 0016690480 scopus 로고
    • 1 complex in the respiratory chain: Protonmotive ubiquinone cycle
    • 1 complex in the respiratory chain: Protonmotive ubiquinone cycle. FEBS Lett. 56, 1-6.
    • (1975) FEBS Lett , vol.56 , pp. 1-6
    • Mitchell, P.1
  • 3
    • 0028277764 scopus 로고
    • The protonmotive Q cycle in mitochondria and bacteria
    • Brandt, U., and Trumpower, B. L. (1994) The protonmotive Q cycle in mitochondria and bacteria. Crit. Rev. Biochem. Mol. Biol. 29, 165-197.
    • (1994) Crit. Rev. Biochem. Mol. Biol , vol.29 , pp. 165-197
    • Brandt, U.1    Trumpower, B.L.2
  • 6
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • Osyczka, A., Moser, C. C., Daldal, F., and Dutton, P. L. (2004) Reversible redox energy coupling in electron transfer chains. Nature 427, 607-612.
    • (2004) Nature , vol.427 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daldal, F.3    Dutton, P.L.4
  • 8
    • 3542991515 scopus 로고    scopus 로고
    • The quinone chemistry of bc complexes
    • Rich, P. R. (2004) The quinone chemistry of bc complexes. Biochim. Biophys. Acta 1658, 165-171.
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 165-171
    • Rich, P.R.1
  • 9
    • 33748913718 scopus 로고    scopus 로고
    • 1 complex: A new gating mechanism that prevents short circuits
    • 1 complex: A new gating mechanism that prevents short circuits. Biochim. Biophys. Acta 1757, 1019-1034.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1019-1034
    • Crofts, A.R.1
  • 10
    • 0016681098 scopus 로고
    • Mitochondrial production of superoxide anions and its relationship to the antymycin insensitive respiration
    • Boveris, A., and Cadenas, E. (1975) Mitochondrial production of superoxide anions and its relationship to the antymycin insensitive respiration. FEBS Lett. 54, 311-314.
    • (1975) FEBS Lett , vol.54 , pp. 311-314
    • Boveris, A.1    Cadenas, E.2
  • 12
    • 0032545269 scopus 로고    scopus 로고
    • Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria
    • Zhang, L., Yu, L., and Yu, C. A. (1998) Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria. J. Biol. Chem. 273, 33972-33976.
    • (1998) J. Biol. Chem , vol.273 , pp. 33972-33976
    • Zhang, L.1    Yu, L.2    Yu, C.A.3
  • 13
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre, J., Buckingham, J. A., Roebuck, S. J., and Brand, M. D. (2002) Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277, 44784-44790.
    • (2002) J. Biol. Chem , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 14
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller, F. L., Liu, Y., and Van Remmen, H. (2004) Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 279, 49064-49073.
    • (2004) J. Biol. Chem , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 15
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria. Central role of complex III
    • Chen, Q., Vazquez, E. J., Moghaddas, S., Hoppel, C. L., and Lesnefsky, E. J. (2003) Production of reactive oxygen species by mitochondria. Central role of complex III. J. Biol. Chem. 278, 36027-36031.
    • (2003) J. Biol. Chem , vol.278 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 16
    • 33747596652 scopus 로고    scopus 로고
    • Oxygen sensing by mitochondria at complex III: The paradox of increased reactive oxygen species during hypoxia
    • Guzy, R. D., and Schumacker, P. T. (2006) Oxygen sensing by mitochondria at complex III: The paradox of increased reactive oxygen species during hypoxia. Exp. Physiol. 91, 807-819.
    • (2006) Exp. Physiol , vol.91 , pp. 807-819
    • Guzy, R.D.1    Schumacker, P.T.2
  • 21
    • 30144441164 scopus 로고    scopus 로고
    • Understanding the cytochrome bc complexes by what they don't do. The Q cycle at 30
    • Cape, J. L., Bowman, M. K., and Kramer, D. M. (2006) Understanding the cytochrome bc complexes by what they don't do. The Q cycle at 30. Trends Plant Sci. 11, 46-55.
    • (2006) Trends Plant Sci , vol.11 , pp. 46-55
    • Cape, J.L.1    Bowman, M.K.2    Kramer, D.M.3
  • 33
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunneling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X., and Dutton, P. L. (1999) Natural engineering principles of electron tunneling in biological oxidation-reduction. Nature 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.