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Volumn 19, Issue 8, 2000, Pages 1777-1783

Supercomplexes in the respiratory chains of yeast and mammalian mitochondria

Author keywords

Blue native PAGE; Complex I; Complex III; Complex IV; F1F0 ATP synthase

Indexed keywords

BINDING PROTEIN; CYTOCHROME C OXIDASE; DIMER; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 0038230469     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.8.1777     Document Type: Article
Times cited : (1113)

References (26)
  • 1
    • 0022375122 scopus 로고
    • The respiratory system of Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium
    • Anemüller, S., Lübben, M. and Schäfer, G. (1985) The respiratory system of Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium. FEBS Lett., 193, 83-87.
    • (1985) FEBS Lett. , vol.193 , pp. 83-87
    • Anemüller, S.1    Lübben, M.2    Schäfer, G.3
  • 4
    • 0032570865 scopus 로고    scopus 로고
    • The respiratory chain in yeast behaves as a single functional unit
    • Boumans, H., Grivell, L.A. and Berden, J.A. (1998) The respiratory chain in yeast behaves as a single functional unit. J. Biol. Chem., 273, 4872-4877.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4872-4877
    • Boumans, H.1    Grivell, L.A.2    Berden, J.A.3
  • 6
    • 0020494216 scopus 로고
    • Arrangement of proteins in the mitochondrial inner membrane
    • Capaldi, R.A. (1982) Arrangement of proteins in the mitochondrial inner membrane. Biochim. Biophys. Acta, 694, 291-306.
    • (1982) Biochim. Biophys. Acta , vol.694 , pp. 291-306
    • Capaldi, R.A.1
  • 8
    • 0038940770 scopus 로고    scopus 로고
    • C- to N-terminal translocation of preproteins into mitochondria
    • Fölsch, H., Gaume, B., Brunner, M., Neupert, W. and Stuart, R.A. (1998) C- to N-terminal translocation of preproteins into mitochondria. EMBO J., 17, 6508-6515.
    • (1998) EMBO J. , vol.17 , pp. 6508-6515
    • Fölsch, H.1    Gaume, B.2    Brunner, M.3    Neupert, W.4    Stuart, R.A.5
  • 9
    • 0000607935 scopus 로고
    • Studies on the electron transfer system
    • Fowler, L.R. and Richardson, H.S. (1963) Studies on the electron transfer system. J. Biol. Chem., 238, 456-463.
    • (1963) J. Biol. Chem. , vol.238 , pp. 456-463
    • Fowler, L.R.1    Richardson, H.S.2
  • 10
    • 0023948895 scopus 로고
    • The role of cytochrome c diffusion in mitochondrial electron transport
    • Gupte, S.S. and Hackenbrock, C.R. (1988) The role of cytochrome c diffusion in mitochondrial electron transport. J. Biol. Chem., 263, 5248-5253.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5248-5253
    • Gupte, S.S.1    Hackenbrock, C.R.2
  • 11
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • Hatefi, Y. (1985) The mitochondrial electron transport and oxidative phosphorylation system. Annu. Rev. Biochem., 54, 1015-1069.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 12
    • 77956996049 scopus 로고
    • The preparation and properties of DPNH-cytochrome c reductase (complex I-III of the respiratory chain)
    • Hatefi, Y. and Rieske, J.S. (1967) The preparation and properties of DPNH-cytochrome c reductase (complex I-III of the respiratory chain). Methods Enzymol., 10, 225-231.
    • (1967) Methods Enzymol. , vol.10 , pp. 225-231
    • Hatefi, Y.1    Rieske, J.S.2
  • 13
    • 0029590774 scopus 로고
    • Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. strain 7. I. The archaeal terminal oxidase supercomplex is a functional fusion of respiratory complexes III and IV with no c-type cytochromes
    • Iwasaki, T., Matsuura, K. and Oshima, T. (1995a) Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. strain 7. I. The archaeal terminal oxidase supercomplex is a functional fusion of respiratory complexes III and IV with no c-type cytochromes. J. Biol. Chem., 270, 30881-30892.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30881-30892
    • Iwasaki, T.1    Matsuura, K.2    Oshima, T.3
  • 14
    • 0029603607 scopus 로고
    • II. Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. strain 7
    • Iwasaki, T., Wakagi, T., Isogai, Y., Iizuka, T. and Oshima, T. (1995b) II. Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. strain 7. J. Biol. Chem., 270, 30893-30901.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30893-30901
    • Iwasaki, T.1    Wakagi, T.2    Isogai, Y.3    Iizuka, T.4    Oshima, T.5
  • 15
    • 0025349462 scopus 로고
    • Coupling site I and the rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles
    • Kotlyar, A.B., Sled, V.D., Burbaev, D.S., Moroz, I.A. and Vinogradov, A.D. (1990) Coupling site I and the rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles. FEBS Lett., 264, 17-20.
    • (1990) FEBS Lett. , vol.264 , pp. 17-20
    • Kotlyar, A.B.1    Sled, V.D.2    Burbaev, D.S.3    Moroz, I.A.4    Vinogradov, A.D.5
  • 16
    • 0015909789 scopus 로고
    • Further evidence for the pool function of ubiquinone as derived from the inhibition of the electron transport by antimycin
    • Kröger, A. and Klingenberg, M. (1973) Further evidence for the pool function of ubiquinone as derived from the inhibition of the electron transport by antimycin. Eur. J. Biochem., 39, 313-323.
    • (1973) Eur. J. Biochem. , vol.39 , pp. 313-323
    • Kröger, A.1    Klingenberg, M.2
  • 17
    • 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
  • 18
    • 0344820721 scopus 로고    scopus 로고
    • Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
    • Okun, J.G., Lümmen, P. and Brandt, U. (1999) Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase). J. Biol. Chem., 274, 2625-2630.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2625-2630
    • Okun, J.G.1    Lümmen, P.2    Brandt, U.3
  • 19
    • 0018087249 scopus 로고
    • The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase
    • Ragan, C.I. and Heron, C. (1978) The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Biochem. J., 174, 783-790.
    • (1978) Biochem. J. , vol.174 , pp. 783-790
    • Ragan, C.I.1    Heron, C.2
  • 20
    • 0021758697 scopus 로고
    • Electron and proton transfer through quinones and cytochrome bc complexes
    • Rich, P.R. (1984) Electron and proton transfer through quinones and cytochrome bc complexes. Biochim. Biophys. Acta, 768, 53-79.
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 53-79
    • Rich, P.R.1
  • 21
    • 0032490099 scopus 로고    scopus 로고
    • Human complex I deficiency: Clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect
    • Robinson, B.H. (1998) Human complex I deficiency: clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect. Biochim. Biophys. Acta, 1364, 271-286.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 271-286
    • Robinson, B.H.1
  • 22
    • 0029013434 scopus 로고
    • Quantification of oxidative phosphorylation enzymes after blue native electrophoresis and two-dimensional resolution: Normal complex I protein amounts in Parkinson's disease conflict with reduced catalytic activities
    • Schägger, H. (1995) Quantification of oxidative phosphorylation enzymes after blue native electrophoresis and two-dimensional resolution: normal complex I protein amounts in Parkinson's disease conflict with reduced catalytic activities. Electrophoresis, 16, 763-770.
    • (1995) Electrophoresis , vol.16 , pp. 763-770
    • Schägger, H.1
  • 23
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger, H. and von Jagow, G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem., 217, 220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schägger, H.1    Von Jagow, G.2
  • 24
    • 0023656799 scopus 로고
    • 1 complex and cytochrome oxidase in the thermophilic bacterium PS3
    • 1 complex and cytochrome oxidase in the thermophilic bacterium PS3. J. Biol. Chem., 262, 15386-15391.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15386-15391
    • Sone, N.1    Sekimachi, M.2    Kutoh, E.3
  • 25
    • 77956984970 scopus 로고
    • Preparation and properties of succinic-cytochrome c reductase (complex II-III)
    • Tisdale, H.D. (1967) Preparation and properties of succinic-cytochrome c reductase (complex II-III). Methods Enzymol., 10, 213-216.
    • (1967) Methods Enzymol. , vol.10 , pp. 213-216
    • Tisdale, H.D.1
  • 26
    • 0032490104 scopus 로고    scopus 로고
    • Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) and pseudo-reversible active/inactive enzyme transition
    • Vinogradov, A.D. (1998) Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) and pseudo-reversible active/inactive enzyme transition. Biochim. Biophys. Acta, 1364, 169-185.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 169-185
    • Vinogradov, A.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.