메뉴 건너뛰기




Volumn 292, Issue 4, 2007, Pages

Kinetics of integrated electron transfer in the mitochondrial respiratory chain: Random collisions vs. solid state electron channeling

Author keywords

Complex I (NADH ubiquinone oxidoreductase); Mitochondria; Supercomplexes; Ubiquinone

Indexed keywords

CARBONATE DEHYDRATASE; CYTOCHROME C; CYTOCHROME C OXIDASE; ELECTRON TRANSFERRING FLAVOPROTEIN; LIPID; MEMBRANE PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINATE DEHYDROGENASE (UBIQUINONE); UBIDECARENONE; UBIQUINOL CYTOCHROME C REDUCTASE; UBIQUINONE;

EID: 34247373746     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00263.2006     Document Type: Review
Times cited : (127)

References (190)
  • 3
    • 1542467765 scopus 로고    scopus 로고
    • The coenzyme Q10 analog decylubiquinone inhibits the redox-activated mitochondrial permeability transition: Role of mitochondrial complex III
    • Armstrong JS, Whiteman M, Rose P, Jones DP. The coenzyme Q10 analog decylubiquinone inhibits the redox-activated mitochondrial permeability transition: role of mitochondrial complex III. J Biol Chem 278: 49079-49084, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 49079-49084
    • Armstrong, J.S.1    Whiteman, M.2    Rose, P.3    Jones, D.P.4
  • 5
    • 34247343391 scopus 로고    scopus 로고
    • Baum H. Coupling between the charge-separating devices of the mitochondrion: intra- or extramembrane. In: The Molecular Biology of Membranes, edited by Fleischer S, Hatefi Y, MacLennan DH, Tzagolff A. New York: Plenum, 1977, p. 243-262.
    • Baum H. Coupling between the charge-separating devices of the mitochondrion: intra- or extramembrane. In: The Molecular Biology of Membranes, edited by Fleischer S, Hatefi Y, MacLennan DH, Tzagolff A. New York: Plenum, 1977, p. 243-262.
  • 6
    • 0026584524 scopus 로고
    • Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses?
    • Beal MF. Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses? Ann Neurol 31: 119-130, 1992.
    • (1992) Ann Neurol , vol.31 , pp. 119-130
    • Beal, M.F.1
  • 7
    • 0015526672 scopus 로고
    • The allosteric binding of antimycin to cytochrome b in the mitochondrial membrane
    • Berden JA, Slater EC. The allosteric binding of antimycin to cytochrome b in the mitochondrial membrane. Biochim Biophys Acta 256: 199-215, 1972.
    • (1972) Biochim Biophys Acta , vol.256 , pp. 199-215
    • Berden, J.A.1    Slater, E.C.2
  • 8
    • 0021918980 scopus 로고
    • Isolation of ubiquinol oxidase from Paracoccus denitrificans and resolution into cytochrome bc1 and cytochrome c-aa3 complexes
    • Berry EA, Trumpower BL. Isolation of ubiquinol oxidase from Paracoccus denitrificans and resolution into cytochrome bc1 and cytochrome c-aa3 complexes. J Biol Chem 260: 2458-2467, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 2458-2467
    • Berry, E.A.1    Trumpower, B.L.2
  • 9
    • 0034693765 scopus 로고    scopus 로고
    • New insight into the structure and function of the alternative oxidase
    • Berthold DA, Andersson ME, Nordlund P. New insight into the structure and function of the alternative oxidase. Biochim Biophys Acta 1460: 241-254, 2000.
    • (2000) Biochim Biophys Acta , vol.1460 , pp. 241-254
    • Berthold, D.A.1    Andersson, M.E.2    Nordlund, P.3
  • 10
    • 0347419384 scopus 로고    scopus 로고
    • Structural and functional organization of Complex I in the mitochondrial respiratory chain
    • Bianchi C, Fato R, Genova ML, Parenti Castelli G, Lenaz G. Structural and functional organization of Complex I in the mitochondrial respiratory chain. Biofactors 18: 3-9, 2003.
    • (2003) Biofactors , vol.18 , pp. 3-9
    • Bianchi, C.1    Fato, R.2    Genova, M.L.3    Parenti Castelli, G.4    Lenaz, G.5
  • 11
    • 4344561983 scopus 로고    scopus 로고
    • The mitochondrial respiratory chain is partially organized in a supercomplex assembly: Kinetic evidence using flux control analysis
    • Bianchi C, Genova ML, Parenti Castelli G, Lenaz G. The mitochondrial respiratory chain is partially organized in a supercomplex assembly: kinetic evidence using flux control analysis. J Biol Chem 279: 36562-36569, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 36562-36569
    • Bianchi, C.1    Genova, M.L.2    Parenti Castelli, G.3    Lenaz, G.4
  • 12
    • 0000836036 scopus 로고
    • Studies on the electron transfer system. LIV. Isolation of the unit electron transfer
    • Blair PV, Oda T, Green DE. Studies on the electron transfer system. LIV. Isolation of the unit electron transfer. Biochemistry 2: 756-764, 1963.
    • (1963) Biochemistry , vol.2 , pp. 756-764
    • Blair, P.V.1    Oda, T.2    Green, D.E.3
  • 13
    • 0025993884 scopus 로고
    • Physical properties of the fluid lipid-bilayer component of cell membranes: A perspective
    • Bloom M, Evans E, Mouritsen OG. Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective. Q Rev Biophys 24: 293-397, 1991.
    • (1991) Q Rev Biophys , vol.24 , pp. 293-397
    • Bloom, M.1    Evans, E.2    Mouritsen, O.G.3
  • 14
    • 0001029550 scopus 로고
    • Subchloroplast fragments: Digitonin method
    • Boardman NK. Subchloroplast fragments: digitonin method. Methods Enzymol 23: 268-276, 1971.
    • (1971) Methods Enzymol , vol.23 , pp. 268-276
    • Boardman, N.K.1
  • 15
    • 0032570865 scopus 로고    scopus 로고
    • The respiratory chain in yeast behaves as a single functional unit
    • Boumans H, Grivell LA, Berden JA. The respiratory chain in yeast behaves as a single functional unit. J Biol Chem 273: 4872-4877, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 4872-4877
    • Boumans, H.1    Grivell, L.A.2    Berden, J.A.3
  • 16
    • 29344439984 scopus 로고    scopus 로고
    • Mitochondrial contact sites: Their role in energy metabolism and apoptosis
    • Brdiczka DG, Zorov DB, Sheu SS. Mitochondrial contact sites: their role in energy metabolism and apoptosis. Biochim Biophys Acta 1762: 148-163, 2006.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 148-163
    • Brdiczka, D.G.1    Zorov, D.B.2    Sheu, S.S.3
  • 17
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown DA, London E. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J Biol Chem 275: 17221-17224, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 18
    • 13544262322 scopus 로고    scopus 로고
    • Bunoust O, Devin A, Avéret N, Camougrand N, Rigoulet M. Competition of electrons to enter the respiratory chain. A new regulatory mechanism of oxidative metabolism in Saccharomyces cerevisiae. J Biol Chem 280: 3407-3413, 2005.
    • Bunoust O, Devin A, Avéret N, Camougrand N, Rigoulet M. Competition of electrons to enter the respiratory chain. A new regulatory mechanism of oxidative metabolism in Saccharomyces cerevisiae. J Biol Chem 280: 3407-3413, 2005.
  • 19
    • 0020494216 scopus 로고
    • Arrangement of proteins in the mitochondrial inner membrane
    • Capaldi RA. Arrangement of proteins in the mitochondrial inner membrane. Biochim Biophys Acta 694: 292-306, 1982.
    • (1982) Biochim Biophys Acta , vol.694 , pp. 292-306
    • Capaldi, R.A.1
  • 20
    • 0001433788 scopus 로고
    • A method for the localization of sites for oxidative phosphorylation
    • Chance B, Williams GR. A method for the localization of sites for oxidative phosphorylation. Nature 176: 250-254, 1955.
    • (1955) Nature , vol.176 , pp. 250-254
    • Chance, B.1    Williams, G.R.2
  • 21
    • 3843147327 scopus 로고    scopus 로고
    • Mitochondrial ATP synthasome: Three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP
    • Chen C, Ko YH, Delannoy M, Ludtke SJ, Chiu W, Pedersen PL. Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP. J Biol Chem 279: 31761-31768, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 31761-31768
    • Chen, C.1    Ko, Y.H.2    Delannoy, M.3    Ludtke, S.J.4    Chiu, W.5    Pedersen, P.L.6
  • 22
    • 2442538306 scopus 로고    scopus 로고
    • Anti-cooperative oxidation of ubiquinol by the yeast cytochrome bc1 complex
    • Covian R, Gutierrez-Cirlos EB, Trumpower BL. Anti-cooperative oxidation of ubiquinol by the yeast cytochrome bc1 complex. J Biol Chem 279: 15040-15049, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 15040-15049
    • Covian, R.1    Gutierrez-Cirlos, E.B.2    Trumpower, B.L.3
  • 24
    • 4244182267 scopus 로고    scopus 로고
    • Crane FL, Widmer C, Lester RL, Hatefi Y. Studies on the electron transport system. XV. Coenzyme Q (Q275) and the succinoxidase activity of the electron transport particle. Biochim Biophys Acta 31: 476-489, 1959.
    • Crane FL, Widmer C, Lester RL, Hatefi Y. Studies on the electron transport system. XV. Coenzyme Q (Q275) and the succinoxidase activity of the electron transport particle. Biochim Biophys Acta 31: 476-489, 1959.
  • 25
    • 0034674060 scopus 로고    scopus 로고
    • The cytochrome bc1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria
    • Cruciat CM, Brunner S, Baumann F, Neupert W, Stuart RA. The cytochrome bc1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria. J Biol Chem 275: 18093-18098, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 18093-18098
    • Cruciat, C.M.1    Brunner, S.2    Baumann, F.3    Neupert, W.4    Stuart, R.A.5
  • 26
    • 0022386485 scopus 로고
    • Substrate channelling of oxalacetate in solid-state complexes of malate dehydrogenase and citrate synthase
    • Datta A, Merz JM, Spivey HO. Substrate channelling of oxalacetate in solid-state complexes of malate dehydrogenase and citrate synthase. J Biol Chem 260: 15008-15012, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 15008-15012
    • Datta, A.1    Merz, J.M.2    Spivey, H.O.3
  • 27
    • 0019644226 scopus 로고
    • Spectroscopic properties of ubiquinones in model systems
    • Degli Esposti M, Ferri E, Lenaz G. Spectroscopic properties of ubiquinones in model systems. Ital J Biochem 30: 437-452, 1981.
    • (1981) Ital J Biochem , vol.30 , pp. 437-452
    • Degli Esposti, M.1    Ferri, E.2    Lenaz, G.3
  • 28
    • 0028050314 scopus 로고
    • Antioxidants and disease prevention
    • Diplock AT. Antioxidants and disease prevention. Mol Aspects Med 15: 293-376, 1994.
    • (1994) Mol Aspects Med , vol.15 , pp. 293-376
    • Diplock, A.T.1
  • 29
    • 85012754084 scopus 로고
    • Probing structure and motion of the mitochondrial cytochromes
    • Dixit BP, Vanderkooi JM. Probing structure and motion of the mitochondrial cytochromes. Curr Top Bioenerg 13: 159-202, 1984.
    • (1984) Curr Top Bioenerg , vol.13 , pp. 159-202
    • Dixit, B.P.1    Vanderkooi, J.M.2
  • 30
    • 33745713601 scopus 로고    scopus 로고
    • Thermodynamic and structural study of the main phospholipid components comprising the mitochondrial inner membrane
    • Domenech O, Sanz F, Montero MT, Hernandez-Borrel J. Thermodynamic and structural study of the main phospholipid components comprising the mitochondrial inner membrane. Biochim Biophys Acta 1758: 213-221, 2006.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 213-221
    • Domenech, O.1    Sanz, F.2    Montero, M.T.3    Hernandez-Borrel, J.4
  • 31
    • 0036035933 scopus 로고    scopus 로고
    • Lipid rafts in mast cell signalling
    • Draber P, Draberova L. Lipid rafts in mast cell signalling. Mol Immunol 38: 1247-1252, 2001.
    • (2001) Mol Immunol , vol.38 , pp. 1247-1252
    • Draber, P.1    Draberova, L.2
  • 32
    • 0021114962 scopus 로고
    • Cross-linking of mitochondrial matrix proteins in situ
    • D'Souza SF, Srere PA. Cross-linking of mitochondrial matrix proteins in situ. Biochim Biophys Acta 724: 40-51, 1983.
    • (1983) Biochim Biophys Acta , vol.724 , pp. 40-51
    • D'Souza, S.F.1    Srere, P.A.2
  • 33
    • 14744270722 scopus 로고    scopus 로고
    • Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III
    • Dudkina NV, Eubel H, Keegstra W, Boekema EJ, Braun HP. Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III. Proc Natl Acad Sci USA 102: 3225-3229, 2005.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3225-3229
    • Dudkina, N.V.1    Eubel, H.2    Keegstra, W.3    Boekema, E.J.4    Braun, H.P.5
  • 34
    • 0034735799 scopus 로고    scopus 로고
    • Coenzyme Q is an obligatory cofactor for uncoupling protein function
    • Echtay KS, Winkler E, Klingenberg M. Coenzyme Q is an obligatory cofactor for uncoupling protein function. Nature 408: 609-613, 2000.
    • (2000) Nature , vol.408 , pp. 609-613
    • Echtay, K.S.1    Winkler, E.2    Klingenberg, M.3
  • 35
    • 8244238712 scopus 로고
    • A partial separation and characterization of cytochrome oxidase and cytochrome b
    • Eichel B, Wainio WW, Person I, Cooperstein SJ. A partial separation and characterization of cytochrome oxidase and cytochrome b. J Biol Chem 183: 89-103, 1950.
    • (1950) J Biol Chem , vol.183 , pp. 89-103
    • Eichel, B.1    Wainio, W.W.2    Person, I.3    Cooperstein, S.J.4
  • 36
    • 0022531708 scopus 로고
    • A milling crowd model for local and long-range obstructed lateral diffusion. Mobility of excimeric probes in the membrane of intact erythrocytes
    • Eisinger J, Flores J, Petersen WP. A milling crowd model for local and long-range obstructed lateral diffusion. Mobility of excimeric probes in the membrane of intact erythrocytes. Biophys J 49: 987-1001, 1986.
    • (1986) Biophys J , vol.49 , pp. 987-1001
    • Eisinger, J.1    Flores, J.2    Petersen, W.P.3
  • 37
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • Ernster L, Dallner G. Biochemical, physiological and medical aspects of ubiquinone function. Biochim Biophys Acta 1271: 195-204, 1995.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 195-204
    • Ernster, L.1    Dallner, G.2
  • 38
    • 0019835356 scopus 로고
    • Mitochondria: A historical review
    • s
    • Ernster L, Schatz G. Mitochondria: a historical review. J Cell Biol 91: 227s-255s, 1981.
    • (1981) J Cell Biol , vol.91
    • Ernster, L.1    Schatz, G.2
  • 40
    • 0027484368 scopus 로고
    • Assay conditions for the mitochondrial NADH:coenzyme Q oxidoreductase
    • Estornell E, Fato R, Pallotti F, Lenaz G. Assay conditions for the mitochondrial NADH:coenzyme Q oxidoreductase. FEBS Lett 332: 127-131, 1993.
    • (1993) FEBS Lett , vol.332 , pp. 127-131
    • Estornell, E.1    Fato, R.2    Pallotti, F.3    Lenaz, G.4
  • 41
    • 1942501850 scopus 로고    scopus 로고
    • Identification and characterization of respirasomes in potato mitochondria
    • Eubel H, Heinemeyer J, Braun HP. Identification and characterization of respirasomes in potato mitochondria. Plant Physiol 134: 1450-1459, 2004.
    • (2004) Plant Physiol , vol.134 , pp. 1450-1459
    • Eubel, H.1    Heinemeyer, J.2    Braun, H.P.3
  • 43
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II
    • Eubel H, Jansch L, Braun HP. New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II. Plant Physiol 133: 274-286, 2003.
    • (2003) Plant Physiol , vol.133 , pp. 274-286
    • Eubel, H.1    Jansch, L.2    Braun, H.P.3
  • 44
    • 0024361268 scopus 로고
    • Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the α-ketoglutarate complex
    • Fahien LA, MacDonald MJ, Teller JK, Fibich B, Fahien CM. Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the α-ketoglutarate complex. J Biol Chem 264: 12303-12312, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 12303-12312
    • Fahien, L.A.1    MacDonald, M.J.2    Teller, J.K.3    Fibich, B.4    Fahien, C.M.5
  • 45
    • 0023040886 scopus 로고
    • Determination of partition and lateral diffusion coefficients of ubiquinones by fluorescence quenching of n-(9-anthroyloxy)stearic acids in phospholipid vesicles and mitochondrial membranes
    • Fato R, Battino M, Degli Esposti M, Parenti Castelli G, Lenaz G. Determination of partition and lateral diffusion coefficients of ubiquinones by fluorescence quenching of n-(9-anthroyloxy)stearic acids in phospholipid vesicles and mitochondrial membranes. Biochemistry 25: 3378-3390, 1986.
    • (1986) Biochemistry , vol.25 , pp. 3378-3390
    • Fato, R.1    Battino, M.2    Degli Esposti, M.3    Parenti Castelli, G.4    Lenaz, G.5
  • 46
    • 0027469526 scopus 로고
    • Steady-state kinetics of ubiquinol-cytochrome c reductase in bovine heart submitochondrial particles: Diffusional effects
    • Fato R, Cavazzoni M, Castelluccio C, Parenti Castelli G, Palmer G, Degli Esposti M, Lenaz G. Steady-state kinetics of ubiquinol-cytochrome c reductase in bovine heart submitochondrial particles: diffusional effects. Biochem J 290: 225-236, 1993.
    • (1993) Biochem J , vol.290 , pp. 225-236
    • Fato, R.1    Cavazzoni, M.2    Castelluccio, C.3    Parenti Castelli, G.4    Palmer, G.5    Degli Esposti, M.6    Lenaz, G.7
  • 47
    • 0029914228 scopus 로고    scopus 로고
    • Steady-state kinetics of the reduction of coenzyme Q analogs by complex I (NADH:ubiquinone oxidoreductase) in bovine heart mitochondria and submitochondrial particles
    • Fato R, Estornell E, Di Bernardo S, Pallotti F, Parenti Castelli G, Lenaz G. Steady-state kinetics of the reduction of coenzyme Q analogs by complex I (NADH:ubiquinone oxidoreductase) in bovine heart mitochondria and submitochondrial particles. Biochemistry 35: 2705-2716, 1996.
    • (1996) Biochemistry , vol.35 , pp. 2705-2716
    • Fato, R.1    Estornell, E.2    Di Bernardo, S.3    Pallotti, F.4    Parenti Castelli, G.5    Lenaz, G.6
  • 48
    • 0003310658 scopus 로고    scopus 로고
    • Fleischer S, Brierley G, Klouwen H, Slautterback DB. Studies of the electron transfer system. 47. The role of phospholipids in electron transfer. J Biol Chem 237: 3264-3272, 1962.
    • Fleischer S, Brierley G, Klouwen H, Slautterback DB. Studies of the electron transfer system. 47. The role of phospholipids in electron transfer. J Biol Chem 237: 3264-3272, 1962.
  • 50
    • 0001693643 scopus 로고
    • A rapid method for the preparation of highly purified cytochrome oxidase
    • Fowler LR, Richardson SH, Hatefi Y. A rapid method for the preparation of highly purified cytochrome oxidase. Biochim Biophys Acta 64: 170-173, 1962.
    • (1962) Biochim Biophys Acta , vol.64 , pp. 170-173
    • Fowler, L.R.1    Richardson, S.H.2    Hatefi, Y.3
  • 51
    • 0024986927 scopus 로고
    • Electron transfer flavoprotein and electron transfer flavoprotein-ubiquinone oxidoreductase
    • Frerman FE. Electron transfer flavoprotein and electron transfer flavoprotein-ubiquinone oxidoreductase. Prog Clin Biol Res 321: 69-77, 1990.
    • (1990) Prog Clin Biol Res , vol.321 , pp. 69-77
    • Frerman, F.E.1
  • 52
    • 0021762595 scopus 로고
    • Cytochrome c-mediated electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase. Kinetic evidence for a mobile cytochrome c pool
    • Froud RJ, Ragan CI. Cytochrome c-mediated electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase. Kinetic evidence for a mobile cytochrome c pool. Biochem J 217: 551-560, 1984.
    • (1984) Biochem J , vol.217 , pp. 551-560
    • Froud, R.J.1    Ragan, C.I.2
  • 53
    • 0019335160 scopus 로고
    • Cardiolipin requirement by cytochrome oxidase and the catalytic role of phospholipid
    • Fry M, Green DE. Cardiolipin requirement by cytochrome oxidase and the catalytic role of phospholipid. Biochem Biophys Res Commun 93: 1238-1246, 1980.
    • (1980) Biochem Biophys Res Commun , vol.93 , pp. 1238-1246
    • Fry, M.1    Green, D.E.2
  • 54
    • 0019887784 scopus 로고
    • Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain
    • Fry M, Green DE. Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain. J Biol Chem 256: 1874-1880, 1981.
    • (1981) J Biol Chem , vol.256 , pp. 1874-1880
    • Fry, M.1    Green, D.E.2
  • 55
    • 34247358373 scopus 로고    scopus 로고
    • Supercomplex organization of the mitochondrial respiratory chain and the role of the Coenzyme Q pool: Pathophysiological implications
    • Genova ML, Bianchi C, Lenaz G. Supercomplex organization of the mitochondrial respiratory chain and the role of the Coenzyme Q pool: pathophysiological implications. Biofactors 23: 1-16, 2006.
    • (2006) Biofactors , vol.23 , pp. 1-16
    • Genova, M.L.1    Bianchi, C.2    Lenaz, G.3
  • 58
    • 0030771336 scopus 로고    scopus 로고
    • Wetting and capillary condensation as means of protein organization in membranes
    • Gil T, Sabra MC, Ipsen JH, Mouritsen OG. Wetting and capillary condensation as means of protein organization in membranes. Biophys J 73: 1728-1741, 1997.
    • (1997) Biophys J , vol.73 , pp. 1728-1741
    • Gil, T.1    Sabra, M.C.2    Ipsen, J.H.3    Mouritsen, O.G.4
  • 59
    • 0027937548 scopus 로고
    • Oxidative stress: Free radical production in neural degeneration
    • Götz ME, Künig G, Riederer P, Youdim MBH. Oxidative stress: free radical production in neural degeneration. Pharmacol Ther 63: 37-122, 1994.
    • (1994) Pharmacol Ther , vol.63 , pp. 37-122
    • Götz, M.E.1    Künig, G.2    Riederer, P.3    Youdim, M.B.H.4
  • 60
    • 26444526806 scopus 로고
    • Studies on the electron transport system. XXXIII. Succinic-cytochrome c reductase
    • Green DE, Burkhard RK. Studies on the electron transport system. XXXIII. Succinic-cytochrome c reductase. Arch Biochem Biophys 92: 312-320, 1961.
    • (1961) Arch Biochem Biophys , vol.92 , pp. 312-320
    • Green, D.E.1    Burkhard, R.K.2
  • 61
    • 0014028935 scopus 로고
    • The mitochondrial electron transfer chain
    • Green DE, Tzagoloff A. The mitochondrial electron transfer chain. Arch Biochem Biophys 116: 293-304, 1966.
    • (1966) Arch Biochem Biophys , vol.116 , pp. 293-304
    • Green, D.E.1    Tzagoloff, A.2
  • 62
    • 0007018201 scopus 로고
    • Stoichiometry of the fixed oxidation-reduction components of the electron transfer chain of beef heart mitochondria
    • Green DE, Wharton DC. Stoichiometry of the fixed oxidation-reduction components of the electron transfer chain of beef heart mitochondria. Biochem Z 338: 335-348, 1963.
    • (1963) Biochem Z , vol.338 , pp. 335-348
    • Green, D.E.1    Wharton, D.C.2
  • 63
    • 0001536888 scopus 로고
    • Studies on the electron transfer system. XXXV. Purification and properties of cytochrome oxidase
    • Griffiths DE, Wharton DC. Studies on the electron transfer system. XXXV. Purification and properties of cytochrome oxidase. J Biol Chem 236: 1850-1856, 1961.
    • (1961) J Biol Chem , vol.236 , pp. 1850-1856
    • Griffiths, D.E.1    Wharton, D.C.2
  • 64
    • 0345059204 scopus 로고    scopus 로고
    • The mitochondrial and prokaryotic proton-translocating NADH: Ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites
    • Grivennikova VG, Roth R, Zakharova NV, Hagerhall C, Vinogradov AD. The mitochondrial and prokaryotic proton-translocating NADH: ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites. Biochim Biophys Acta 1607: 79-90, 2003.
    • (2003) Biochim Biophys Acta , vol.1607 , pp. 79-90
    • Grivennikova, V.G.1    Roth, R.2    Zakharova, N.V.3    Hagerhall, C.4    Vinogradov, A.D.5
  • 65
    • 0023889649 scopus 로고
    • Multidimensional diffusion modes and collision frequencies of cytochrome c with its redox partners
    • Gupte SS, Hackenbrock CR. Multidimensional diffusion modes and collision frequencies of cytochrome c with its redox partners. J Biol Chem 263: 5241-5247, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 5241-5247
    • Gupte, S.S.1    Hackenbrock, C.R.2
  • 66
    • 0023948895 scopus 로고
    • The role of cytochrome c diffusion in mitochondrial electron transport
    • Gupte SS, Hackenbrock CR. The role of cytochrome c diffusion in mitochondrial electron transport. J Biol Chem 263: 5248-5253, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 5248-5253
    • Gupte, S.S.1    Hackenbrock, C.R.2
  • 67
    • 0021430791 scopus 로고
    • Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidationreduction components
    • Gupte SS, Wu ES, Hoechli L, Hoechli M, Jacobson K, Sowers AE, Hackenbrock CR. Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidationreduction components. Proc Natl Acad Sci USA 81: 2606-2610, 1984.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 2606-2610
    • Gupte, S.S.1    Wu, E.S.2    Hoechli, L.3    Hoechli, M.4    Jacobson, K.5    Sowers, A.E.6    Hackenbrock, C.R.7
  • 68
    • 0001771591 scopus 로고
    • Kinetic analysis of electron flux through the quinones in the mitochondrial system
    • edited by Lenaz G. Chichester, UK: Wiley
    • Gutman M. Kinetic analysis of electron flux through the quinones in the mitochondrial system. In: Coenzyme Q, edited by Lenaz G. Chichester, UK: Wiley, 1985, p. 215-234.
    • (1985) Coenzyme Q , pp. 215-234
    • Gutman, M.1
  • 69
    • 0015409372 scopus 로고
    • Mutual inhibition between NADH oxidase and succinoxidase activities in respiring submitochondrial particles
    • Gutman M, Silman N. Mutual inhibition between NADH oxidase and succinoxidase activities in respiring submitochondrial particles. FEBS Lett 26: 207-210, 1972.
    • (1972) FEBS Lett , vol.26 , pp. 207-210
    • Gutman, M.1    Silman, N.2
  • 70
    • 0023052462 scopus 로고
    • Spin-label electron paramagnetic resonance and differential scanning calorimetry studies of the interaction between mitochondrial succinate-ubiquinone and ubiquinol-cytochrome c reductases
    • Gwak SH, Yu L, Yu CA. Spin-label electron paramagnetic resonance and differential scanning calorimetry studies of the interaction between mitochondrial succinate-ubiquinone and ubiquinol-cytochrome c reductases. Biochemistry 25: 7675-7682, 1986.
    • (1986) Biochemistry , vol.25 , pp. 7675-7682
    • Gwak, S.H.1    Yu, L.2    Yu, C.A.3
  • 71
    • 0022790702 scopus 로고
    • The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
    • Hackenbrock CR, Chazotte B, Gupte SS. The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport. J Bioenerg Biomembr 18: 331-368, 1986.
    • (1986) J Bioenerg Biomembr , vol.18 , pp. 331-368
    • Hackenbrock, C.R.1    Chazotte, B.2    Gupte, S.S.3
  • 72
    • 0016695208 scopus 로고
    • Cytochrome c oxidase in liver mitochondria
    • Hackenbrock CR, Hammon KM. Cytochrome c oxidase in liver mitochondria. J Biol Chem 250: 9185-9187, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 9185-9187
    • Hackenbrock, C.R.1    Hammon, K.M.2
  • 73
    • 0018113861 scopus 로고
    • Preparation and properties of the enzymes and enzymes complexes of the mitochondrial oxidative phosphorylation system
    • Hatefi Y. Preparation and properties of the enzymes and enzymes complexes of the mitochondrial oxidative phosphorylation system. Methods Enzymol 53: 3, 1978.
    • (1978) Methods Enzymol , vol.53 , pp. 3
    • Hatefi, Y.1
  • 74
    • 78651138333 scopus 로고
    • Studies on the electron transfer system. XLII. Reconstitution of the electron transfer system
    • Hatefi Y, Haavik AG, Fowler LR, Griffiths DE. Studies on the electron transfer system. XLII. Reconstitution of the electron transfer system. J Biol Chem 237: 2661-2669, 1962.
    • (1962) J Biol Chem , vol.237 , pp. 2661-2669
    • Hatefi, Y.1    Haavik, A.G.2    Fowler, L.R.3    Griffiths, D.E.4
  • 75
    • 0000948392 scopus 로고
    • Studies on the electron transfer system. XL. Preparation and properties of mitochondrial DPNH-Coenzyme Q reductase
    • Hatefi Y, Haavik AG, Griffiths DE. Studies on the electron transfer system. XL. Preparation and properties of mitochondrial DPNH-Coenzyme Q reductase. J Biol Chem 237: 1676-1680, 1962.
    • (1962) J Biol Chem , vol.237 , pp. 1676-1680
    • Hatefi, Y.1    Haavik, A.G.2    Griffiths, D.E.3
  • 76
    • 0001060105 scopus 로고    scopus 로고
    • Hatefi Y, Haavik AG, Griffiths DE. Studies on the electron transfer system. XLI. Reduced Coenzyme Q (QH2)-cytochrome c reductase. J Biol Chem 237: 1681-1685, 1962.
    • Hatefi Y, Haavik AG, Griffiths DE. Studies on the electron transfer system. XLI. Reduced Coenzyme Q (QH2)-cytochrome c reductase. J Biol Chem 237: 1681-1685, 1962.
  • 77
    • 0008308755 scopus 로고
    • Studies on the electron transfer system. XXX. DPNH cytochrome c reductase I
    • Hatefi Y, Haavik AG, Jurtshuck P. Studies on the electron transfer system. XXX. DPNH cytochrome c reductase I. Biochim Biophys Acta 52: 106-118, 1961.
    • (1961) Biochim Biophys Acta , vol.52 , pp. 106-118
    • Hatefi, Y.1    Haavik, A.G.2    Jurtshuck, P.3
  • 78
    • 34247357951 scopus 로고
    • Studies on the electron transport system. XVI. Enzymic oxidoreduction reactions of coenzyme Q
    • Hatefi Y, Lest RL, Crane FL, Widmer C. Studies on the electron transport system. XVI. Enzymic oxidoreduction reactions of coenzyme Q. Biochim Biophys Acta 31: 490-501, 1959.
    • (1959) Biochim Biophys Acta , vol.31 , pp. 490-501
    • Hatefi, Y.1    Lest, R.L.2    Crane, F.L.3    Widmer, C.4
  • 79
    • 0018790727 scopus 로고
    • The effects of lipid phase transitions on the interaction of mitochondrial NADH-ubiquinone oxidoreductase with ubiquinol-cytochrome c oxidoreductase
    • Heron C, Gore MG, Ragan CI. The effects of lipid phase transitions on the interaction of mitochondrial NADH-ubiquinone oxidoreductase with ubiquinol-cytochrome c oxidoreductase. Biochem J 178: 415-426, 1979.
    • (1979) Biochem J , vol.178 , pp. 415-426
    • Heron, C.1    Gore, M.G.2    Ragan, C.I.3
  • 80
    • 0018171433 scopus 로고
    • The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase: Restoration of ubiquinone-pool behaviour
    • Heron C, Ragan CI, Trumpower BL. The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase: restoration of ubiquinone-pool behaviour. Biochem J 174: 791-800, 1978.
    • (1978) Biochem J , vol.174 , pp. 791-800
    • Heron, C.1    Ragan, C.I.2    Trumpower, B.L.3
  • 82
    • 0018342081 scopus 로고
    • Lateral translational diffusion of cytochrome c oxidase in the mitochondrial energy-transducing membrane
    • Hochli M, Hackenbrock CR,. Lateral translational diffusion of cytochrome c oxidase in the mitochondrial energy-transducing membrane. Proc Natl Acad Sci USA 76: 1236-1240, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 1236-1240
    • Hochli, M.1    Hackenbrock, C.R.2
  • 83
    • 0021815336 scopus 로고
    • Mobility in the mitochondrial electron transport chain
    • Hochman J, Ferguson Miller S, Schindler M. Mobility in the mitochondrial electron transport chain. Biochemistry 24: 2509-2516, 1985.
    • (1985) Biochemistry , vol.24 , pp. 2509-2516
    • Hochman, J.1    Ferguson Miller, S.2    Schindler, M.3
  • 85
    • 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, Oshima T. 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.
    • (1995) J Biol Chem , vol.270 , pp. 30881-30892
    • Iwasaki, T.1    Matsuura, K.2    Oshima, T.3
  • 86
    • 0018823799 scopus 로고
    • Pyrimidine nucleotide biosynthsis in animals. Genes, enzymes and regulation of UMP biosynthesis
    • Jones ME. Pyrimidine nucleotide biosynthsis in animals. Genes, enzymes and regulation of UMP biosynthesis. Annu Rev Biochem 49: 253-279, 1980.
    • (1980) Annu Rev Biochem , vol.49 , pp. 253-279
    • Jones, M.E.1
  • 88
    • 0018527496 scopus 로고
    • Molecular democracy: Who shares the controls?
    • Kacser A, Burns JA. Molecular democracy: who shares the controls? Biochem Soc Trans 7: 1149-1160, 1979.
    • (1979) Biochem Soc Trans , vol.7 , pp. 1149-1160
    • Kacser, A.1    Burns, J.A.2
  • 89
    • 0018799845 scopus 로고
    • Nuclear magnetic resonance investigation of the cytochrome oxidase-phospholipid interaction: A new model for boundary lipid
    • Kang SY, Gutowsky HS, Hsung JC, Jacobs R, King TE, Rice D, Oldfield E. Nuclear magnetic resonance investigation of the cytochrome oxidase-phospholipid interaction: a new model for boundary lipid. Biochemistry 18: 3257-3267, 1979.
    • (1979) Biochemistry , vol.18 , pp. 3257-3267
    • Kang, S.Y.1    Gutowsky, H.S.2    Hsung, J.C.3    Jacobs, R.4    King, T.E.5    Rice, D.6    Oldfield, E.7
  • 90
    • 0019888239 scopus 로고
    • Rotation of cytochrome oxidase in phospholipid vesicles. Investigations of interactions between cytochrome oxidases and between cytochrome oxidase and cytochrome bc1 complex
    • Kawato S, Sigel E, Carafoli E, Cherry RJ. Rotation of cytochrome oxidase in phospholipid vesicles. Investigations of interactions between cytochrome oxidases and between cytochrome oxidase and cytochrome bc1 complex. J Biol Chem 256: 7518-7527, 1981.
    • (1981) J Biol Chem , vol.256 , pp. 7518-7527
    • Kawato, S.1    Sigel, E.2    Carafoli, E.3    Cherry, R.J.4
  • 91
    • 0034663640 scopus 로고    scopus 로고
    • Diversity and origin of alternative NADH:ubiquinone oxidoreductases
    • Kerscher SJ. Diversity and origin of alternative NADH:ubiquinone oxidoreductases. Biochim Biophys Acta 1459: 274-283, 2000.
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 274-283
    • Kerscher, S.J.1
  • 92
    • 0027456261 scopus 로고
    • Metabolic channelling and control of the flux
    • Kholodenko NB, Westerhoff HV. Metabolic channelling and control of the flux. FEBS Lett 320: 71-74, 1993.
    • (1993) FEBS Lett , vol.320 , pp. 71-74
    • Kholodenko, N.B.1    Westerhoff, H.V.2
  • 93
    • 2842612138 scopus 로고
    • Iron, copper, cytochrome, and lipid contents of heart muscle preparation and heart mitochondria
    • King TE, Nickel KS, Jensen DR. Iron, copper, cytochrome, and lipid contents of heart muscle preparation and heart mitochondria. J Biol Chem 239: 1989-1994, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 1989-1994
    • King, T.E.1    Nickel, K.S.2    Jensen, D.R.3
  • 94
    • 0014764841 scopus 로고
    • Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane
    • Klingenberg M. Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane. Eur J Biochem 13: 247-252, 1970.
    • (1970) Eur J Biochem , vol.13 , pp. 247-252
    • Klingenberg, M.1
  • 95
    • 0020490571 scopus 로고
    • The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications
    • Koppenol WH, Margoliash E. The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications. J Biol Chem 257: 4426-4437, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 4426-4437
    • Koppenol, W.H.1    Margoliash, E.2
  • 96
    • 2442599389 scopus 로고    scopus 로고
    • Absence of NADH channelling in coupled reaction of mitochondrial malate dehydrogenase and Complex I in alamethicin-permeabilized rat liver mitochondria
    • Kotlyar AB, Maklashina E, Cecchini G. Absence of NADH channelling in coupled reaction of mitochondrial malate dehydrogenase and Complex I in alamethicin-permeabilized rat liver mitochondria. Biochem Biophys Res Commun 318: 987-991, 2004.
    • (2004) Biochem Biophys Res Commun , vol.318 , pp. 987-991
    • Kotlyar, A.B.1    Maklashina, E.2    Cecchini, G.3
  • 99
    • 2942700102 scopus 로고    scopus 로고
    • Supramolecular organization of cytochrome c oxidase- and alternative oxidase-dependent respiratory chains in the filamentous fungus Podospora anserine
    • Krause F, Scheckhuber CQ, Werner A, Rexroth S, Reifschneider NH, Dencher NA, Osiewacz HD. Supramolecular organization of cytochrome c oxidase- and alternative oxidase-dependent respiratory chains in the filamentous fungus Podospora anserine. J Biol Chem 279: 26453-26461, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 26453-26461
    • Krause, F.1    Scheckhuber, C.Q.2    Werner, A.3    Rexroth, S.4    Reifschneider, N.H.5    Dencher, N.A.6    Osiewacz, H.D.7
  • 100
    • 0015607377 scopus 로고
    • The kinetics of the redox reactions of ubiquinone related to the electron-transport activity in the respiratory chain
    • Kröger A, Klingenberg M. The kinetics of the redox reactions of ubiquinone related to the electron-transport activity in the respiratory chain. Eur J Biochem 34: 358-368, 1973.
    • (1973) Eur J Biochem , vol.34 , pp. 358-368
    • Kröger, A.1    Klingenberg, M.2
  • 101
    • 0015909789 scopus 로고
    • Further evidence of the pool function of ubiquinone as derived from the inhibition of the electron transport by antimycin
    • Kröger A, Klingenberg M. Further evidence of the pool function of ubiquinone as derived from the inhibition of the electron transport by antimycin. Eur J Biochem 39: 313-323, 1973.
    • (1973) Eur J Biochem , vol.39 , pp. 313-323
    • Kröger, A.1    Klingenberg, M.2
  • 102
    • 0035803487 scopus 로고    scopus 로고
    • Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure
    • Lange C, Nett JH, Trumpower BL, Hunte C. Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure. EMBO J 20: 6591-6600, 2001.
    • (2001) EMBO J , vol.20 , pp. 6591-6600
    • Lange, C.1    Nett, J.H.2    Trumpower, B.L.3    Hunte, C.4
  • 103
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • Lee AG. How lipids affect the activities of integral membrane proteins. Biochim Biophys Acta 1666: 62-87, 2004.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 104
    • 0001442551 scopus 로고
    • Identification of the ubiquinone-binding domain in QPs1 of succinate-ubiquinone reductase
    • Lee GY, He DY, Yu L, Yu CA. Identification of the ubiquinone-binding domain in QPs1 of succinate-ubiquinone reductase. J Biol Chem 270: 6193-6198, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 6193-6198
    • Lee, G.Y.1    He, D.Y.2    Yu, L.3    Yu, C.A.4
  • 105
    • 0023680684 scopus 로고
    • Role of mobility of redox components in the inner mitochondrial membrane
    • Lenaz G. Role of mobility of redox components in the inner mitochondrial membrane. J Membr Biol 104: 193-209, 1988.
    • (1988) J Membr Biol , vol.104 , pp. 193-209
    • Lenaz, G.1
  • 106
    • 0032504657 scopus 로고    scopus 로고
    • Role of mitochondria in oxidative stress and ageing
    • Lenaz G. Role of mitochondria in oxidative stress and ageing. Biochim Biophys Acta 1366: 53-67, 1998.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 53-67
    • Lenaz, G.1
  • 109
    • 0002127403 scopus 로고
    • A survey of the function and specificity of Ubiquinone in the mitochondrial respiratory chain
    • edited by Lenaz G. Chichester, UK: Wiley
    • Lenaz G, De Santis A, Bertoli E. A survey of the function and specificity of Ubiquinone in the mitochondrial respiratory chain. In: Coenzyme Q, edited by Lenaz G. Chichester, UK: Wiley, 1985, p. 165-200.
    • (1985) Coenzyme Q , pp. 165-200
    • Lenaz, G.1    De Santis, A.2    Bertoli, E.3
  • 110
    • 0022790638 scopus 로고
    • Is ubiquinone diffusion rate-limiting for electron transfer?
    • Lenaz G, Fato R. Is ubiquinone diffusion rate-limiting for electron transfer? J Bioenerg Biomembr 18: 369-401, 1986.
    • (1986) J Bioenerg Biomembr , vol.18 , pp. 369-401
    • Lenaz, G.1    Fato, R.2
  • 112
    • 0029002718 scopus 로고
    • Underevaluation of complex I activity by the direct assay of NADH-coenzyme Q reductase in rat liver mitochondria
    • Lenaz G, Fato R, Genova ML, Formiggini G, Parenti Castelli G, Bovina C. Underevaluation of complex I activity by the direct assay of NADH-coenzyme Q reductase in rat liver mitochondria. FEBS Lett 366: 119-121, 1995.
    • (1995) FEBS Lett , vol.366 , pp. 119-121
    • Lenaz, G.1    Fato, R.2    Genova, M.L.3    Formiggini, G.4    Parenti Castelli, G.5    Bovina, C.6
  • 114
    • 0022974883 scopus 로고
    • Choline oxidation and choline dehydrogenase
    • Lin CS, Wu RD. Choline oxidation and choline dehydrogenase. J Protein Chem 5: 193-200, 1986.
    • (1986) J Protein Chem , vol.5 , pp. 193-200
    • Lin, C.S.1    Wu, R.D.2
  • 115
    • 0028053707 scopus 로고
    • Metabolic studies on Saccharomyces cerevisiae containing fused citrate synthase/malate dehydrogenase
    • Lindbladh C, Brodeur RD, Small WC, Lilius G, Bulow L, Mosbach K, Srere PA. Metabolic studies on Saccharomyces cerevisiae containing fused citrate synthase/malate dehydrogenase. Biochemistry 33: 11684-11691, 1994.
    • (1994) Biochemistry , vol.33 , pp. 11684-11691
    • Lindbladh, C.1    Brodeur, R.D.2    Small, W.C.3    Lilius, G.4    Bulow, L.5    Mosbach, K.6    Srere, P.A.7
  • 116
    • 0028151319 scopus 로고
    • Preparation and kinetic characterization of a fusion protein of yeast mitochondrial citrate synthase and malate dehydrogenase
    • Lindbladh C, Rault M, Hagglund C, Small WC, Mosbach K, Bulow L, Evans C, Srere PA. Preparation and kinetic characterization of a fusion protein of yeast mitochondrial citrate synthase and malate dehydrogenase. Biochemistry 33: 11692-11698, 1994.
    • (1994) Biochemistry , vol.33 , pp. 11692-11698
    • Lindbladh, C.1    Rault, M.2    Hagglund, C.3    Small, W.C.4    Mosbach, K.5    Bulow, L.6    Evans, C.7    Srere, P.A.8
  • 117
    • 0014028069 scopus 로고
    • Studies on the mechanism of oxidative phosphorylation. IX(-X). Effect of cytochrome c on energylinked processes (-in submitochondrial particles)
    • MacLennan DH, Lenaz G, Szarkowska L. Studies on the mechanism of oxidative phosphorylation. IX(-X). Effect of cytochrome c on energylinked processes (-in submitochondrial particles). J Biol Chem 241: 5251-5265, 1966.
    • (1966) J Biol Chem , vol.241 , pp. 5251-5265
    • MacLennan, D.H.1    Lenaz, G.2    Szarkowska, L.3
  • 118
    • 29344434866 scopus 로고    scopus 로고
    • The relevance of mitochondrial membrane topology to mitochondrial function
    • Mannella CA. The relevance of mitochondrial membrane topology to mitochondrial function. Biochim Biophys Acta 1762: 140-147, 2006.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 140-147
    • Mannella, C.A.1
  • 119
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
    • Marsh D, Horvath LI. Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling. Biochim Biophys Acta 1376: 267-296, 1998.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 267-296
    • Marsh, D.1    Horvath, L.I.2
  • 120
    • 0141629674 scopus 로고    scopus 로고
    • EPR studies of phospholipid bilayers after lipoperoxidation. 1. Inner molecular order and fluidity gradient
    • Megli FM, Sabatini K. EPR studies of phospholipid bilayers after lipoperoxidation. 1. Inner molecular order and fluidity gradient. Chem Phys Lipids 125: 161-172, 2003.
    • (2003) Chem Phys Lipids , vol.125 , pp. 161-172
    • Megli, F.M.1    Sabatini, K.2
  • 122
    • 0038311752 scopus 로고    scopus 로고
    • A new dawn for plant mitochondrial NAD(P)H dehydrogenases
    • Møller IM. A new dawn for plant mitochondrial NAD(P)H dehydrogenases. Trends Plant Sci 7: 235-237, 2002.
    • (2002) Trends Plant Sci , vol.7 , pp. 235-237
    • Møller, I.M.1
  • 123
    • 0000047526 scopus 로고    scopus 로고
    • Determining and understanding the control of flux. An illustration in submitochondrial particles of how to validate schemes of metabolic control
    • Moreno-Sanchez R, Bravo C, Westerhoff HV. Determining and understanding the control of flux. An illustration in submitochondrial particles of how to validate schemes of metabolic control. Eur J Biochem 264: 427-433, 1999.
    • (1999) Eur J Biochem , vol.264 , pp. 427-433
    • Moreno-Sanchez, R.1    Bravo, C.2    Westerhoff, H.V.3
  • 124
    • 0032491445 scopus 로고    scopus 로고
    • Interaction between citrate synthase and malate dehydrogenase. Substrate channelling of oxaloacetate
    • Morgunov I, Srere PA. Interaction between citrate synthase and malate dehydrogenase. Substrate channelling of oxaloacetate. J Biol Chem 273: 29540-29544, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 29540-29544
    • Morgunov, I.1    Srere, P.A.2
  • 125
    • 0027172336 scopus 로고
    • Comparison of ubiquinol and cytochrome c terminal oxidases. An alternative view
    • Musser SM, Stowell MHB, Chan SI. Comparison of ubiquinol and cytochrome c terminal oxidases. An alternative view. FEBS Lett 327: 131-136, 1993.
    • (1993) FEBS Lett , vol.327 , pp. 131-136
    • Musser, S.M.1    Stowell, M.H.B.2    Chan, S.I.3
  • 126
    • 0016288208 scopus 로고
    • Studies with ubiquinonedepleted submitochondrial particles. Quantitative incorporation of small amounts of ubiquinone and its effects on the NADH and succinate oxidase activities
    • Norling B, Glazek E, . Nelson BD, Ernster L. Studies with ubiquinonedepleted submitochondrial particles. Quantitative incorporation of small amounts of ubiquinone and its effects on the NADH and succinate oxidase activities. Eur J Biochem 47: 475-482, 1974.
    • (1974) Eur J Biochem , vol.47 , pp. 475-482
    • Norling, B.1    Glazek, E.2    Nelson, B.D.3    Ernster, L.4
  • 127
    • 0022836506 scopus 로고
    • A difference infrared-spectroscopic study of the interaction of ubiquinone-10 with phospholipid bilayers
    • Ondarroa V, Quinn PJ. A difference infrared-spectroscopic study of the interaction of ubiquinone-10 with phospholipid bilayers. Biochem J 240: 325-331, 1986.
    • (1986) Biochem J , vol.240 , pp. 325-331
    • Ondarroa, V.1    Quinn, P.J.2
  • 128
    • 0028674909 scopus 로고
    • Binding of malate dehydrogenase and NADH channelling to complex I
    • Ovadi J, Huang Y, Spivey HO. Binding of malate dehydrogenase and NADH channelling to complex I. Mol Recognit 7: 265-272, 1994.
    • (1994) Mol Recognit , vol.7 , pp. 265-272
    • Ovadi, J.1    Huang, Y.2    Spivey, H.O.3
  • 129
    • 0029847843 scopus 로고    scopus 로고
    • Metabolic consequences of enzyme interactions
    • Ovadi J, Srere PA. Metabolic consequences of enzyme interactions. Cell Biochem Funct 14: 249-258, 1996.
    • (1996) Cell Biochem Funct , vol.14 , pp. 249-258
    • Ovadi, J.1    Srere, P.A.2
  • 130
    • 0030897739 scopus 로고    scopus 로고
    • Genetic and functional changes in mitochondria associated with aging
    • Ozawa T. Genetic and functional changes in mitochondria associated with aging. Physiol Rev 77: 425-464, 1997.
    • (1997) Physiol Rev , vol.77 , pp. 425-464
    • Ozawa, T.1
  • 131
    • 34247379198 scopus 로고    scopus 로고
    • Ozawa T, Nishikimi M, Suzuki H, Tanaka M, Shimomura Y. Structure and assembly of mitochondrial electron-transfer complexes. In: Bioenergetics: Structure and Function of Energy-Transducing Systems, edited by Ozawa T, Papa S. Tokyo: Japan Sci. Soc., 1987, p. 101-119.
    • Ozawa T, Nishikimi M, Suzuki H, Tanaka M, Shimomura Y. Structure and assembly of mitochondrial electron-transfer complexes. In: Bioenergetics: Structure and Function of Energy-Transducing Systems, edited by Ozawa T, Papa S. Tokyo: Japan Sci. Soc., 1987, p. 101-119.
  • 132
    • 0346059551 scopus 로고    scopus 로고
    • Decrease in mitochondrial complex I. activity in ischemic/ reperfused rat heart: Involvement of reactive oxygen species and cardiolipin
    • Paradies G, Petrosillo G, Pistolese M, Di Venosa N, Federici A, Ruggiero FM. Decrease in mitochondrial complex I. activity in ischemic/ reperfused rat heart: involvement of reactive oxygen species and cardiolipin. Circ Res 94: 53-59, 2004.
    • (2004) Circ Res , vol.94 , pp. 53-59
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Di Venosa, N.4    Federici, A.5    Ruggiero, F.M.6
  • 133
    • 0033984710 scopus 로고    scopus 로고
    • The effect of reactive oxygen species generated from the mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles
    • Paradies G, Petrosillo G, Pistolese M, Ruggiero FM. The effect of reactive oxygen species generated from the mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles. FEBS Lett 466: 323-326, 2000.
    • (2000) FEBS Lett , vol.466 , pp. 323-326
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 134
    • 0037029129 scopus 로고    scopus 로고
    • Reactive oxygen species affect mitochondrial electron transport complex I. activity through oxidative cardiolipin damage
    • Paradies G, Petrosillo G, Pistolese M, Ruggiero FM,. Reactive oxygen species affect mitochondrial electron transport complex I. activity through oxidative cardiolipin damage. Gene 286: 135-141, 2002.
    • (2002) Gene , vol.286 , pp. 135-141
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 135
    • 33746100806 scopus 로고
    • Kinetic studies on the pool function of ubiquinone in mitochondrial systems
    • Parenti Castelli G, Fato R, Castelluccio C, Lenaz G. Kinetic studies on the pool function of ubiquinone in mitochondrial systems. Chem Scr 27: 161-166, 1987.
    • (1987) Chem Scr , vol.27 , pp. 161-166
    • Parenti Castelli, G.1    Fato, R.2    Castelluccio, C.3    Lenaz, G.4
  • 136
    • 0034141634 scopus 로고    scopus 로고
    • Preliminary evidence for the existence of specific functional assemblies between enzymes of the β-oxidation pathway and the respiratory chain
    • Parker A, Engel PC. Preliminary evidence for the existence of specific functional assemblies between enzymes of the β-oxidation pathway and the respiratory chain. Biochem J 345: 429-435, 2000.
    • (2000) Biochem J , vol.345 , pp. 429-435
    • Parker, A.1    Engel, P.C.2
  • 137
    • 0037387920 scopus 로고    scopus 로고
    • Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: Role of reactive oxygen species and cardiolipin
    • Petrosillo G, Ruggiero FM, Di Venosa N, Paradies G. Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: role of reactive oxygen species and cardiolipin. FASEB J 17: 714-716, 2003.
    • (2003) FASEB J , vol.17 , pp. 714-716
    • Petrosillo, G.1    Ruggiero, F.M.2    Di Venosa, N.3    Paradies, G.4
  • 139
    • 33744987954 scopus 로고    scopus 로고
    • Control by cytochrome c oxidase of the cellular oxidative phosphorylation system depends on the mitochondrial energy state
    • Piccoli C, Scrima R, Boffoli D, Capitanio N. Control by cytochrome c oxidase of the cellular oxidative phosphorylation system depends on the mitochondrial energy state. Biochem J 396: 573-583, 2006.
    • (2006) Biochem J , vol.396 , pp. 573-583
    • Piccoli, C.1    Scrima, R.2    Boffoli, D.3    Capitanio, N.4
  • 140
    • 0026766756 scopus 로고
    • Spin-label electron paramagnetic resonance and differential scanning calorimetry studies of the interaction between mitochondrial cytochrome c oxidase and adenosine triphosphate synthase complex
    • Qiu ZH, Yu L, Yu CA. Spin-label electron paramagnetic resonance and differential scanning calorimetry studies of the interaction between mitochondrial cytochrome c oxidase and adenosine triphosphate synthase complex. Biochemistry 31: 3297-3302, 1992.
    • (1992) Biochemistry , vol.31 , pp. 3297-3302
    • Qiu, Z.H.1    Yu, L.2    Yu, C.A.3
  • 141
    • 46549100769 scopus 로고
    • The kinetics of quinone pools in electron transport
    • Ragan CI, Cottingham IR. The kinetics of quinone pools in electron transport. Biochim Biophys Acta 811: 13-31, 1985.
    • (1985) Biochim Biophys Acta , vol.811 , pp. 13-31
    • Ragan, C.I.1    Cottingham, I.R.2
  • 142
    • 0018087249 scopus 로고
    • The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase: Evidence for stoichiometric association
    • Ragan CI, Heron C. The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase: evidence for stoichiometric association. Biochem J 174: 783-790, 1978.
    • (1978) Biochem J , vol.174 , pp. 783-790
    • Ragan, C.I.1    Heron, C.2
  • 143
    • 0024594990 scopus 로고
    • Synthesis, location, and lateral mobility of fluorescently labeled ubiquinone 10 in mitochondrial and artificial membranes
    • Rajarathnam K, Hochman J, Schindler M, Ferguson-Miller S. Synthesis, location, and lateral mobility of fluorescently labeled ubiquinone 10 in mitochondrial and artificial membranes. Biochemistry 28: 3168-3176, 1989.
    • (1989) Biochemistry , vol.28 , pp. 3168-3176
    • Rajarathnam, K.1    Hochman, J.2    Schindler, M.3    Ferguson-Miller, S.4
  • 144
  • 145
    • 0026723743 scopus 로고
    • Coenzyme Q pool function in glycerol-3-phosphate oxidation in hamster brown adipose tissue mitochondria
    • Rauchova H, Battino M, Fato R, Lenaz G, Drahota Z. Coenzyme Q pool function in glycerol-3-phosphate oxidation in hamster brown adipose tissue mitochondria. J Bioenerg Biomembr 24: 235-241, 1992.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 235-241
    • Rauchova, H.1    Battino, M.2    Fato, R.3    Lenaz, G.4    Drahota, Z.5
  • 146
    • 0021758697 scopus 로고
    • Electron and proton transfers through quinones and bc complexes
    • Rich PR. Electron and proton transfers through quinones and bc complexes. Biochim Biophys Acta 768: 53-79, 1984.
    • (1984) Biochim Biophys Acta , vol.768 , pp. 53-79
    • Rich, P.R.1
  • 147
    • 0034668852 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins: From mitochondria to the regulation of energy balance
    • Ricquier D, Bouillaud F. Mitochondrial uncoupling proteins: from mitochondria to the regulation of energy balance. J Physiol 529: 3-10, 2000.
    • (2000) J Physiol , vol.529 , pp. 3-10
    • Ricquier, D.1    Bouillaud, F.2
  • 148
    • 77956985297 scopus 로고
    • Preparation and properties of reduced coenzyme Q-cytochrome c reductase (complex III of the respiratory chain)
    • Rieske JS. Preparation and properties of reduced coenzyme Q-cytochrome c reductase (complex III of the respiratory chain). Methods Enzymol 10: 239-245, 1967.
    • (1967) Methods Enzymol , vol.10 , pp. 239-245
    • Rieske, J.S.1
  • 149
    • 0022233869 scopus 로고
    • Organization of Krebs tricarboxylic acid cycle enzymes in mitochondria
    • Robinson JB, Srere PA. Organization of Krebs tricarboxylic acid cycle enzymes in mitochondria. J Biol Chem 260: 10800-10880, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 10800-10880
    • Robinson, J.B.1    Srere, P.A.2
  • 150
    • 0019317502 scopus 로고
    • Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation
    • Robinson NC, Strey F, Talbert L. Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation. Biochemistry 19: 3656-3661, 1980.
    • (1980) Biochemistry , vol.19 , pp. 3656-3661
    • Robinson, N.C.1    Strey, F.2    Talbert, L.3
  • 151
    • 0032953969 scopus 로고    scopus 로고
    • Contribution of mitochondrial proton leak to respiration rate in working skeletal muscle and liver and to SMR
    • Rolfe DF, Newman JM, Buckingham JA, Clark MG, Brand MD. Contribution of mitochondrial proton leak to respiration rate in working skeletal muscle and liver and to SMR. Am J Physiol Cell Physiol 276: C692-C696, 1999.
    • (1999) Am J Physiol Cell Physiol , vol.276
    • Rolfe, D.F.1    Newman, J.M.2    Buckingham, J.A.3    Clark, M.G.4    Brand, M.D.5
  • 152
    • 0000282961 scopus 로고
    • Brownian motion in biological membranes
    • Saffman PG, Delbruck M. Brownian motion in biological membranes. Proc Natl Acad Sci USA 72: 3111-3113, 1975.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3111-3113
    • Saffman, P.G.1    Delbruck, M.2
  • 154
    • 0036139981 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes
    • Schägger H. Respiratory chain supercomplexes. IUBMB Life 52: 119-128, 2001.
    • (2001) IUBMB Life , vol.52 , pp. 119-128
    • Schägger, H.1
  • 155
    • 4344630010 scopus 로고    scopus 로고
    • Significance of respirasomes for the assembly/stability of human respiratory chain complex I
    • Schägger H, de Coo R, Bauer MF, Hofmann S, Godinot C, Brandt U. Significance of respirasomes for the assembly/stability of human respiratory chain complex I. J Biol Chem 279: 36349-36353, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 36349-36353
    • Schägger, H.1    de Coo, R.2    Bauer, M.F.3    Hofmann, S.4    Godinot, C.5    Brandt, U.6
  • 156
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger H, Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J 19: 1777-1783, 2000.
    • (2000) EMBO J , vol.19 , pp. 1777-1783
    • Schägger, H.1    Pfeiffer, K.2
  • 157
    • 0035851099 scopus 로고    scopus 로고
    • The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes
    • Schägger H, Pfeiffer K. The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes. J Biol Chem 276: 37861-37867, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 37861-37867
    • Schägger, H.1    Pfeiffer, K.2
  • 158
    • 0020491098 scopus 로고
    • Lateral diffusion of ubiquinone during electron transfer in phospholipid- and ubiquinone-enriched mitochondrial membranes
    • Schneider H, Lemasters JJ, Hackenbrock CR. Lateral diffusion of ubiquinone during electron transfer in phospholipid- and ubiquinone-enriched mitochondrial membranes. J Biol Chem 257: 10789-10793, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 10789-10793
    • Schneider, H.1    Lemasters, J.J.2    Hackenbrock, C.R.3
  • 159
    • 0022628376 scopus 로고
    • Molecular architecture of the inner membrane of mitochondria from rat liver: A combined biochemical and stereological study
    • Schwerzmann K, Cruz-Orive LM, Eggman R, Sänger A, Weibel ER. Molecular architecture of the inner membrane of mitochondria from rat liver: a combined biochemical and stereological study. J Cell Biol 102: 97-103, 1986.
    • (1986) J Cell Biol , vol.102 , pp. 97-103
    • Schwerzmann, K.1    Cruz-Orive, L.M.2    Eggman, R.3    Sänger, A.4    Weibel, E.R.5
  • 160
    • 0033539647 scopus 로고    scopus 로고
    • 2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure
    • 2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure. Biochemistry 8: 14966-14972, 1999.
    • (1999) Biochemistry , vol.8 , pp. 14966-14972
    • Sedlak, E.1    Robinson, N.C.2
  • 161
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature 387: 569-572, 1997.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 162
    • 34247390819 scopus 로고
    • Purification of cytochrome oxidase
    • Smith L, Stotz E. Purification of cytochrome oxidase. J Biol Chem 209: 819-828, 1954.
    • (1954) J Biol Chem , vol.209 , pp. 819-828
    • Smith, L.1    Stotz, E.2
  • 163
    • 0023656799 scopus 로고
    • Identification and properties of a quinol oxidase super-complex composed of a bc1 complex and cytochrome oxidase in the thermophilic bacterium PS3
    • Sone N, Sekimachi M, Kutoh E. Identification and properties of a quinol oxidase super-complex composed of a bc1 complex and cytochrome oxidase in the thermophilic bacterium PS3. J Biol Chem 262: 15386-15391, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 15386-15391
    • Sone, N.1    Sekimachi, M.2    Kutoh, E.3
  • 164
    • 0019770975 scopus 로고
    • Rate of lateral diffusion of intramembrane particles: Measurement by electrophoretic displacement and rerandomization
    • Sowers E, Hackenbrock CR. Rate of lateral diffusion of intramembrane particles: measurement by electrophoretic displacement and rerandomization. Proc Natl Acad Sci USA 78: 6246-6250, 1981.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 6246-6250
    • Sowers, E.1    Hackenbrock, C.R.2
  • 165
    • 0022379631 scopus 로고
    • Variation in protein lateral diffusion coefficients is related to variation in protein concentration found in mitochondrial inner membranes
    • Sowers E, Hackenbrock CR. Variation in protein lateral diffusion coefficients is related to variation in protein concentration found in mitochondrial inner membranes. Biochim Biophys Acta 821: 85-90, 1985.
    • (1985) Biochim Biophys Acta , vol.821 , pp. 85-90
    • Sowers, E.1    Hackenbrock, C.R.2
  • 166
    • 0024654065 scopus 로고
    • Metabolic compartmentation
    • Spivey HO, Merz JM. Metabolic compartmentation. Bioassays 10: 127-130, 1989.
    • (1989) Bioassays , vol.10 , pp. 127-130
    • Spivey, H.O.1    Merz, J.M.2
  • 167
    • 49049142313 scopus 로고
    • The structure of the mitochondrial inner membrane-matrix compartment
    • Srere PA. The structure of the mitochondrial inner membrane-matrix compartment. TIBS 7: 375-378, 1982.
    • (1982) TIBS , vol.7 , pp. 375-378
    • Srere, P.A.1
  • 168
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere PA. Complexes of sequential metabolic enzymes. Annu Rev Biochem 56: 89-124, 1987.
    • (1987) Annu Rev Biochem , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 169
    • 27144457343 scopus 로고    scopus 로고
    • Functional consequences of oxidative membrane damage
    • Stark G. Functional consequences of oxidative membrane damage. J Membr Biol 205: 1-16, 2005.
    • (2005) J Membr Biol , vol.205 , pp. 1-16
    • Stark, G.1
  • 170
    • 0021735199 scopus 로고
    • On the localization of ubiquinone in phosphatidylcholine bilayers
    • Stidham MA, McIntosh TJ, Siedow JN. On the localization of ubiquinone in phosphatidylcholine bilayers. Biochim Biophys Acta 767: 423-431, 1984.
    • (1984) Biochim Biophys Acta , vol.767 , pp. 423-431
    • Stidham, M.A.1    McIntosh, T.J.2    Siedow, J.N.3
  • 171
    • 0021264942 scopus 로고
    • Steady-state kinetics of the overall oxidative phosphorylation reaction in heart mitochondria. Determination of the coupling relationships between the respiratory reactions and miscellaneous observations concerning rate-limiting steps
    • Stoner B. Steady-state kinetics of the overall oxidative phosphorylation reaction in heart mitochondria. Determination of the coupling relationships between the respiratory reactions and miscellaneous observations concerning rate-limiting steps. Bioenerg Biomembr 16: 115-141, 1984.
    • (1984) Bioenerg Biomembr , vol.16 , pp. 115-141
    • Stoner, B.1
  • 172
    • 1042278126 scopus 로고    scopus 로고
    • Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans
    • Stroh A, Anderka O, Pfeiffer K, Yagi T, Finel M, Ludwig, Schägger BH. Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans. J Biol Chem 279: 5000-5007, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 5000-5007
    • Stroh, A.1    Anderka, O.2    Pfeiffer, K.3    Yagi, T.4    Finel, M.5    Ludwig6    Schägger, B.H.7
  • 173
    • 0026012964 scopus 로고
    • Kinetic advantage of the interaction between the fatty acid beta-oxidation enzymes and the complexes of the respiratory chain
    • Sumegi B, Porpaczy Z, Alkonyi I. Kinetic advantage of the interaction between the fatty acid beta-oxidation enzymes and the complexes of the respiratory chain. Biochim Biophys Acta 1081: 121-128, 1991.
    • (1991) Biochim Biophys Acta , vol.1081 , pp. 121-128
    • Sumegi, B.1    Porpaczy, Z.2    Alkonyi, I.3
  • 174
    • 0021744544 scopus 로고
    • Complex I binds several mitochondrial NADcoupled dehydrogenases
    • Sumegi B, Srere PA. Complex I binds several mitochondrial NADcoupled dehydrogenases. J Biol Chem 259: 15040-15045, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 15040-15045
    • Sumegi, B.1    Srere, P.A.2
  • 176
    • 34247339021 scopus 로고
    • Reconstitution of respiratory-enzyme systems. VII. Preparation of the cytochrome b-c1 complex from heart muscle
    • Takemori S, King TE. Reconstitution of respiratory-enzyme systems. VII. Preparation of the cytochrome b-c1 complex from heart muscle. Biochim Biophys Acta 64: 192-194, 1962.
    • (1962) Biochim Biophys Acta , vol.64 , pp. 192-194
    • Takemori, S.1    King, T.E.2
  • 177
    • 0007972619 scopus 로고    scopus 로고
    • Takemori S, King TE. Reconstitution of respiratory chain enzyme systems. 13. Sequential fragmentation of succinate oxidase: preparation of succinate oxidase: preparation and properties of succinate-cytochrome c reductase and the cytochrome b-c1 particle. J Biol Chem 239: 3546-3558, 1964.
    • Takemori S, King TE. Reconstitution of respiratory chain enzyme systems. 13. Sequential fragmentation of succinate oxidase: preparation of succinate oxidase: preparation and properties of succinate-cytochrome c reductase and the cytochrome b-c1 particle. J Biol Chem 239: 3546-3558, 1964.
  • 178
    • 0019558007 scopus 로고
    • New concepts on the role of ubiquinone in the mitochondrial respiratory chain
    • Trumpower BL. New concepts on the role of ubiquinone in the mitochondrial respiratory chain. J Bioenerg Biomembr 13: 1-24, 1981.
    • (1981) J Bioenerg Biomembr , vol.13 , pp. 1-24
    • Trumpower, B.L.1
  • 179
    • 34247378348 scopus 로고    scopus 로고
    • Vanderkooi G. Organization of protein and lipid components in membranes. In: Molecular Biology of Membranes, edited by Fleischer S, Hatefi Y, MacLennan D, Tzagoloff A. New York: Plenum, 1978, p. 25-55.
    • Vanderkooi G. Organization of protein and lipid components in membranes. In: Molecular Biology of Membranes, edited by Fleischer S, Hatefi Y, MacLennan D, Tzagoloff A. New York: Plenum, 1978, p. 25-55.
  • 180
    • 0040777075 scopus 로고    scopus 로고
    • Model of a quinary structure between Krebs TCA cycle enzymes: A model fort the metabolon
    • Vélot C, Mixon MB, Teige M, Srere PA. Model of a quinary structure between Krebs TCA cycle enzymes: a model fort the metabolon. Biochemistry 36: 14271-14276, 1997.
    • (1997) Biochemistry , vol.36 , pp. 14271-14276
    • Vélot, C.1    Mixon, M.B.2    Teige, M.3    Srere, P.A.4
  • 181
    • 0017567464 scopus 로고
    • Lipid requirements for cytochrome c oxidase activity
    • Vik SB, Capaldi RA. Lipid requirements for cytochrome c oxidase activity. Biochemistry 16: 5755-5759, 1977.
    • (1977) Biochemistry , vol.16 , pp. 5755-5759
    • Vik, S.B.1    Capaldi, R.A.2
  • 183
    • 34247334740 scopus 로고
    • The reaction between cytochrome oxidase and ferrocytochrome c
    • Wainio WW, Person P, Eichel B, Cooperstein SJ. The reaction between cytochrome oxidase and ferrocytochrome c. J Biol Chem 192: 349-360, 1951.
    • (1951) J Biol Chem , vol.192 , pp. 349-360
    • Wainio, W.W.1    Person, P.2    Eichel, B.3    Cooperstein, S.J.4
  • 184
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging and cancer: A dawn for evolutionary medicine
    • Wallace DC. A mitochondrial paradigm of metabolic and degenerative diseases, aging and cancer: a dawn for evolutionary medicine. Annu Rev Genet 39: 359-407, 2005.
    • (2005) Annu Rev Genet , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 185
    • 0036554572 scopus 로고    scopus 로고
    • Regulation of the mitochondrial permeability transition pore by ubiquinone analogs. A progress report
    • Walter L, Miyoshi H, Leverve X, Bernard P, Fontaine E. Regulation of the mitochondrial permeability transition pore by ubiquinone analogs. A progress report. Free Radic Res 36: 405-412, 2002.
    • (2002) Free Radic Res , vol.36 , pp. 405-412
    • Walter, L.1    Miyoshi, H.2    Leverve, X.3    Bernard, P.4    Fontaine, E.5
  • 186
    • 0000744663 scopus 로고
    • Studies on cytochrome oxidase. I. Absolute and difference absorption spectra
    • Yonetani T. Studies on cytochrome oxidase. I. Absolute and difference absorption spectra. J Biol Chem 235: 845-852, 1960.
    • (1960) J Biol Chem , vol.235 , pp. 845-852
    • Yonetani, T.1
  • 187
    • 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 A, 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: 409-420, 1980.
    • (1980) Biochim Biophys Acta , vol.591 , pp. 409-420
    • Yu, A.1    Yu, L.2
  • 188
    • 0016168992 scopus 로고
    • Soluble cytochrome b-c1 complex and the reconstitution of succinate-cytochrome c reductase
    • Yu A, Yu L, King TE. Soluble cytochrome b-c1 complex and the reconstitution of succinate-cytochrome c reductase. J Biol Chem 249: 4905-4910, 1974.
    • (1974) J Biol Chem , vol.249 , pp. 4905-4910
    • Yu, A.1    Yu, L.2    King, T.E.3
  • 189
    • 0037113864 scopus 로고    scopus 로고
    • Gluing the respiratory chain together
    • Zhang M, Mileykovskaya E, Dowhan W. Gluing the respiratory chain together. J Biol Chem 277: 43553-43556, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 43553-43556
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.