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Volumn 456, Issue A, 2009, Pages 459-473

Chapter 25 Analysis of Electron Transfer and Superoxide Generation in the Cytochrome bc1 Complex

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMYCIN A1; CHLORIDE; PROTEINASE K; SUPEROXIDE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 63449125904     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)04425-X     Document Type: Review
Times cited : (9)

References (38)
  • 1
    • 0028277764 scopus 로고
    • The proton-motive Q cycle in mitochondria and bacteria
    • Brandt U., and Trumpower B. The proton-motive Q cycle in mitochondria and bacteria. Crit. Rev. Biochem. Mol. Biol. 29 (1994) 165-197
    • (1994) Crit. Rev. Biochem. Mol. Biol. , vol.29 , pp. 165-197
    • Brandt, U.1    Trumpower, B.2
  • 3
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., and Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59 (1979) 527-605
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 4
    • 1942447877 scopus 로고    scopus 로고
    • 1 complex: Function in the context of structure
    • 1 complex: Function in the context of structure. Ann. Rev. Physiol. 66 (2004) 689-733
    • (2004) Ann. Rev. Physiol. , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 5
    • 0029052070 scopus 로고
    • Desferrioxamine inhibition of the hydroxyl radical-like reactivity of peroxynitrite: Role of the hydroxamic groups
    • Denicola A., Souza J.M., Gatti R.M., Augusto O., and Radi R. Desferrioxamine inhibition of the hydroxyl radical-like reactivity of peroxynitrite: Role of the hydroxamic groups. Free Radic. Biol. Med. 19 (1995) 11-19
    • (1995) Free Radic. Biol. Med. , vol.19 , pp. 11-19
    • Denicola, A.1    Souza, J.M.2    Gatti, R.M.3    Augusto, O.4    Radi, R.5
  • 6
    • 0019877746 scopus 로고
    • A new species of bound ubisemiquinone anion in QH2: Cytochrome c oxidoreductase
    • De Vries S., Albracht S.P., Berden J.A., and Slater E.C. A new species of bound ubisemiquinone anion in QH2: Cytochrome c oxidoreductase. J. Biol. Chem. 256 (1981) 11996-11998
    • (1981) J. Biol. Chem. , vol.256 , pp. 11996-11998
    • De Vries, S.1    Albracht, S.P.2    Berden, J.A.3    Slater, E.C.4
  • 11
    • 0001506921 scopus 로고
    • 32p adenosine triphosphate exchange
    • 32p adenosine triphosphate exchange. J. Biol. Chem. 246 (1971) 5477-5487
    • (1971) J. Biol. Chem. , vol.246 , pp. 5477-5487
    • Kagawa, Y.1    Racker, E.2
  • 13
    • 0033858360 scopus 로고    scopus 로고
    • The contribution of mitochondrial respiratory complexes to the production of reactive oxygen species
    • Mclennan H.R., and Esposti M.D. The contribution of mitochondrial respiratory complexes to the production of reactive oxygen species. J. Bioenerg. Biomembr. 32 (2000) 152-162
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 152-162
    • Mclennan, H.R.1    Esposti, M.D.2
  • 14
    • 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
  • 18
    • 0025075792 scopus 로고
    • Determination of superoxide radical and singlet oxygen based on chemiluminescence of luciferin analogs
    • Nakano M. Determination of superoxide radical and singlet oxygen based on chemiluminescence of luciferin analogs. Methods Enzymol. 186 (1990) 585-591
    • (1990) Methods Enzymol. , vol.186 , pp. 585-591
    • Nakano, M.1
  • 19
    • 0022495724 scopus 로고
    • The mitochondrial site of superoxide formation
    • Nohl H., and Jordan W. The mitochondrial site of superoxide formation. Biochem. Bioph. Res. Co. 138 (1986) 533-539
    • (1986) Biochem. Bioph. Res. Co. , vol.138 , pp. 533-539
    • Nohl, H.1    Jordan, W.2
  • 23
    • 0034686023 scopus 로고    scopus 로고
    • 1 complex from Rhodobacter sphaeroides: Location of regions essential for interaction with the three-subunit core complex
    • 1 complex from Rhodobacter sphaeroides: Location of regions essential for interaction with the three-subunit core complex. J. Biol. Chem. 275 (2000) 15287-15294
    • (2000) J. Biol. Chem. , vol.275 , pp. 15287-15294
    • Tso, S.C.1    Shenoy, S.K.2    Quinn, B.N.3    Yu, L.4    Yu, C.A.5
  • 24
    • 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., and 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
  • 25
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens J.F., and Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191 (1980) 421-427
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 26
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens J.F., Alexandre A., and Lehninger A.L. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237 (1985) 408-414
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 27
    • 0027426028 scopus 로고
    • • - production, in vitro, from Kupffer cells stimulated by phorbol myristate acetate
    • • - production, in vitro, from Kupffer cells stimulated by phorbol myristate acetate. FEBS Lett. 335 (1993) 167-170
    • (1993) FEBS Lett. , vol.335 , pp. 167-170
    • Uehara, K.1    Maruyama, N.2    Huang, C.K.3    Nakano, M.4
  • 31
    • 0016610627 scopus 로고
    • Studies on cytochrome oxidase. Interactions of the cytochrome oxidase protein with phospholipids and cytochrome c
    • Yu C.A., Yu L., and King T.E. Studies on cytochrome oxidase. Interactions of the cytochrome oxidase protein with phospholipids and cytochrome c. J. Biol. Chem. 250 (1975) 1383-1392
    • (1975) J. Biol. Chem. , vol.250 , pp. 1383-1392
    • Yu, C.A.1    Yu, L.2    King, T.E.3
  • 32
    • 0019319538 scopus 로고
    • Resolution and reconstitution of succinate-cytochrome c reductase: Preparations and properties of high purity succinate dehydrogenase and ubiquinol-cytochrome c reductase
    • Yu C.A., and Yu L. Resolution and reconstitution of succinate-cytochrome c reductase: Preparations and properties of high purity succinate dehydrogenase and ubiquinol-cytochrome c reductase. Biochim. Biophys. Acta 591 (1980) 409-420
    • (1980) Biochim. Biophys. Acta , vol.591 , pp. 409-420
    • Yu, C.A.1    Yu, L.2
  • 33
    • 0020370722 scopus 로고
    • Synthesis of biologically active ubiquinone derivatives
    • Yu C.A., and Yu L. Synthesis of biologically active ubiquinone derivatives. Biochemistry 21 (1982) 4096-4101
    • (1982) Biochemistry , vol.21 , pp. 4096-4101
    • Yu, C.A.1    Yu, L.2
  • 36
    • 0025767785 scopus 로고
    • Crystallization of mitochondria ubiquinol-cytochrome c reductase
    • Yue W.H., Zou Y.P., Yu L., and Yu C.A. Crystallization of mitochondria ubiquinol-cytochrome c reductase. Biochemistry 30 (1991) 2303-2306
    • (1991) Biochemistry , vol.30 , pp. 2303-2306
    • Yue, W.H.1    Zou, Y.P.2    Yu, L.3    Yu, C.A.4
  • 37
    • 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. Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria. J. Biol. Chem. 273 (1998) 33972-33976
    • (1998) J. Biol. Chem. , vol.273 , pp. 33972-33976
    • Zhang, L.1    Yu, L.2    Yu, C.A.3


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