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Volumn , Issue , 2000, Pages 5-28

Mobility of coenzyme Q in membranes

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EID: 85027258458     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (112)
  • 1
    • 0000587252 scopus 로고
    • Isolation of a quinone from beef heart mitochondria
    • Crane, F. L., Isolation of a quinone from beef heart mitochondria, Biochim. Biophys. Acta, 1000, 358, 1989.
    • (1989) Biochim. Biophys. Acta , vol.1000 , pp. 358
    • Crane, F.L.1
  • 2
    • 0030823103 scopus 로고    scopus 로고
    • The diversity of coenzyme q function
    • Crane, F. L. and Navas, P., The diversity of coenzyme Q function, Molec. Aspects Med., 8, s1-s6, 1997.
    • (1997) Molec. Aspects Med , vol.8 , pp. s1-s6
    • Crane, F.L.1    Navas, P.2
  • 3
    • 0027973899 scopus 로고
    • The role of ascorbate in antioxidant protection in biomembranes. Interaction with vitamin e and coenzyme q
    • Beyer, R. E., The role of ascorbate in antioxidant protection in biomembranes. Interaction with vitamin E and Coenzyme Q, J. Bioenerg. Biomembr., 26, 349, 1994.
    • (1994) J. Bioenerg. Biomembr , vol.26 , pp. 349
    • Beyer, R.E.1
  • 4
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • Ernster, L. and Dallner, G., Biochemical, physiological and medical aspects of ubiquinone function, Biochim. Biophys. Acta, 1271, 195, 1995.
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 195
    • Ernster, L.1    Dallner, G.2
  • 5
    • 0026531457 scopus 로고
    • Succinate-ubiquinone reductase linked recycling of alpha-tocopherol in reconstituted systems and mitochondria: Requirement for reduced ubiquinone
    • Maguire, J. J., Kagan, V, Ackrell, B. A., Serbinova, E., and Packer, L., Succinate-ubiquinone reductase linked recycling of alpha-tocopherol in reconstituted systems and mitochondria: requirement for reduced ubiquinone, Arch. Biochem. Biophys., 292, 47, 1992.
    • (1992) Arch. Biochem. Biophys , vol.292 , pp. 47
    • Maguire, J.J.1    Kagan, V.2    Ackrell, B.A.3    Serbinova, E.4    Packer, L.5
  • 6
    • 0022625444 scopus 로고
    • Rates of membrane-associated reactions: Reduction of dimensionality revisited
    • McCloskey, M. and Poo, M. M., Rates of membrane-associated reactions: reduction of dimensionality revisited, J. Cell Biol., 102, 88, 1986.
    • (1986) J. Cell Biol , vol.102 , pp. 88
    • McCloskey, M.1    Poo, M.M.2
  • 8
    • 0000282961 scopus 로고
    • Brownian motion in biological membranes
    • Saffman, P. G. and Delbrück, M., Brownian motion in biological membranes, Proc. Natl. Acad. Sci., USA, 72, 3111, 1975.
    • (1975) Proc. Natl. Acad. Sci , vol.72 , pp. 3111
    • Saffman, P.G.1    Delbrück, M.2
  • 9
    • 33749224012 scopus 로고
    • Molecular transport in liquids and glasses
    • Cohen, M. H. and Turnbull, D., Molecular transport in liquids and glasses, J. Chem. Phys., 31, 1164, 1959.
    • (1959) J. Chem. Phys , vol.31 , pp. 1164
    • Cohen, M.H.1    Turnbull, D.2
  • 10
    • 0018676644 scopus 로고
    • On two-dimensional passive random walk in lipid bilayers and fluid pathways in biomembranes
    • Galla, H. J., Hartmann, W., Theilen, V, and Sackmann, E., On two-dimensional passive random walk in lipid bilayers and fluid pathways in biomembranes, J. Membr. Biol., 48, 215, 1979.
    • (1979) J. Membr. Biol , vol.48 , pp. 215
    • Galla, H.J.1    Hartmann, W.2    Theilen, V.3    Sackmann, E.4
  • 11
    • 0017752553 scopus 로고
    • Deuterium magnetic resonance: Theory and application to lipid membranes, q
    • Seelig, J., Deuterium magnetic resonance: theory and application to lipid membranes, Q. Rev. Biophys., 10, 353, 1977.
    • (1977) Rev. Biophys , vol.10 , pp. 353
    • Seelig, J.1
  • 12
    • 0004232671 scopus 로고
    • Princeton Univ. Press., Princeton, NJ
    • Berg, H. C., Random Walks in Biology, Princeton Univ. Press., Princeton, NJ, 1984.
    • (1984) Random Walks in Biology
    • Berg, H.C.1
  • 13
    • 0018797528 scopus 로고
    • Rotational and lateral diffusion of membrane proteins
    • Cherry, R. J., Rotational and lateral diffusion of membrane proteins, Biochim. Biophys. Acta, 559, 289, 1979.
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 289
    • Cherry, R.J.1
  • 14
    • 0020144768 scopus 로고
    • Diffusion of molecules on biological membranes of nonplanar form. A theoretical study
    • Aizenbud, B. M. and Gerston, N. D., Diffusion of molecules on biological membranes of nonplanar form. A theoretical study, Biophys. J., 38, 287, 1982.
    • (1982) Biophys. J , vol.38 , pp. 287
    • Aizenbud, B.M.1    Gerston, N.D.2
  • 15
    • 0022790702 scopus 로고
    • The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
    • Hackenbrock, C. R., Chazotte, B., and Gupte, S. S., The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport, J. Bioenerg. Biomembr., 18, 331, 1986.
    • (1986) J. Bioenerg. Biomembr , vol.18 , pp. 331
    • Hackenbrock, C.R.1    Chazotte, B.2    Gupte, S.S.3
  • 17
    • 0012050693 scopus 로고
    • Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: Experimental test of the saffman-delbrück equations
    • Peters, R. and Cherry, R. J., Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: Experimental test of the Saffman-Delbrück equations, Proc. Natl. Acad. Sci., USA, 79, 4317, 1982.
    • (1982) Proc. Natl. Acad. Sci , vol.79 , pp. 4317
    • Peters, R.1    Cherry, R.J.2
  • 19
    • 84910428327 scopus 로고
    • Low frequency and diffuse motion in aligned phospholipid multilayers studied by pulsed nmr
    • Cornell, B. A. and Pope, S. M., Low frequency and diffuse motion in aligned phospholipid multilayers studied by pulsed NMR, Chem. Phys. Lipids, 27, 151, 1980.
    • (1980) Chem. Phys. Lipids , vol.27 , pp. 151
    • Cornell, B.A.1    Pope, S.M.2
  • 20
    • 0018814426 scopus 로고
    • Chlorinated hydrocarbon-cell membrane interactions studied by the fluorescence quenching of carbazole-labeled phospholipids: Probe synthesis and characterization of the quenching methodology
    • Lakowicz, J. R. and Hogen, D., Chlorinated hydrocarbon-cell membrane interactions studied by the fluorescence quenching of carbazole-labeled phospholipids: probe synthesis and characterization of the quenching methodology, Chem. Phys. Lipids, 26, 1, 1981.
    • (1981) Chem. Phys. Lipids , vol.26 , pp. 1
    • Lakowicz, J.R.1    Hogen, D.2
  • 21
    • 0022790638 scopus 로고
    • Is ubiquinone diffusion rate-limiting for electron transfer?
    • Lenaz, G. and Fato, R., Is ubiquinone diffusion rate-limiting for electron transfer?, J. Bioenerg. Biomembr., 18, 369, 1986.
    • (1986) J. Bioenerg. Biomembr , vol.18 , pp. 369
    • Lenaz, G.1    Fato, R.2
  • 23
    • 85052181000 scopus 로고
    • Lateral mobility of proteins in membranes
    • Benga, CRC Press, Boca Raton FL
    • Peters, R., Lateral mobility of proteins in membranes, in Structure and Properties of Cell Membranes, Benga, CRC Press, Boca Raton FL, 1985, 35.
    • (1985) Structure and Properties of Cell Membranes , pp. 35
    • Peters, R.1
  • 24
    • 0017287098 scopus 로고
    • Transmembrane control of the receptors on normal and tumor cells. I. Cytoplasmic influence over surface components
    • Nicolson, G. L., Transmembrane control of the receptors on normal and tumor cells. I. Cytoplasmic influence over surface components, Biochim. Biophys. Acta, 457, 57, 1976.
    • (1976) Biochim. Biophys. Acta , vol.457 , pp. 57
    • Nicolson, G.L.1
  • 25
    • 0019871853 scopus 로고
    • Translational mobility of glucophorin in bilayer membranes of dimyristoylphosphatidylcholine
    • Vaz, W. L. C., Kapitza, H. G., Stümpel, J., Sackmann, E., and Jovin, T. M., Translational Mobility of Glucophorin in Bilayer Membranes of Dimyristoylphosphatidylcholine, Biochemistry, 20, 1392, 1981.
    • (1981) Biochemistry , vol.20 , pp. 1392
    • Vaz, W.L.C.1    Kapitza, H.G.2    Stümpel, J.3    Sackmann, E.4    Jovin, T.M.5
  • 27
    • 0020106881 scopus 로고
    • Quantitative characterization of the lateral distribution of membrane proteins within the lipid bilayer
    • Freire, E. and Snyder, B., Quantitative characterization of the lateral distribution of membrane proteins within the lipid bilayer, Biophys. J., 37, 627, 1982.
    • (1982) Biophys. J , vol.37 , pp. 627
    • Freire, E.1    Snyder, B.2
  • 28
    • 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., and Petersen, W. P, 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, 1986.
    • (1986) Biophys. J , vol.49 , pp. 987
    • Eisinger, J.1    Flores, J.2    Petersen, W.P.3
  • 29
    • 0027931206 scopus 로고
    • Heterogeneity of microsomal membrane fluidity: Evaluation using intrinsic tryptophan energy transfer to pyrene probes
    • Engelke, M., Behmann, T., Ojeda, F., and Diehl, H. A., Heterogeneity of microsomal membrane fluidity: evaluation using intrinsic tryptophan energy transfer to pyrene probes, Chem. Phys. Lipids, 72, 35, 1994.
    • (1994) Chem. Phys. Lipids , vol.72 , pp. 35
    • Engelke, M.1    Behmann, T.2    Ojeda, F.3    Diehl, H.A.4
  • 30
    • 0028584124 scopus 로고
    • Influence of obstacles on lipid lateral diffusion: Computer simulation of frap experiments and application to proteoliposomes and biomembranes
    • Schram, V, Tocanne, J. F., and Lopez, A., Influence of obstacles on lipid lateral diffusion: computer simulation of FRAP experiments and application to proteoliposomes and biomembranes, Eur. Biophys. J., 23, 337, 1994.
    • (1994) Eur. Biophys. J , vol.23 , pp. 337
    • Schram, V.1    Tocanne, J.F.2    Lopez, A.3
  • 31
    • 0017664223 scopus 로고
    • Physics of chemoreception
    • Berg, H. C. and Purcell, E. M., Physics of chemoreception, Biophys. J., 20, 193, 1977.
    • (1977) Biophys. J , vol.20 , pp. 193
    • Berg, H.C.1    Purcell, E.M.2
  • 32
    • 0003064682 scopus 로고
    • Reduction of dimensionality in biological diffusion processes
    • Rich & Davidson, Freeman, San Francisco
    • Adam G. and Delbrück M., Reduction of dimensionality in biological diffusion processes, Structural Chemistry and Molecular Biology, Rich & Davidson, Freeman, San Francisco, 1968, 198.
    • (1968) Structural Chemistry and Molecular Biology , pp. 198
    • Adam, G.1    Delbrück, M.2
  • 34
    • 0000267310 scopus 로고
    • Versuch einer mathematischen theorie der koagulationskinetik kolloider lösungen
    • Smoluchowski, V M., Versuch einer mathematischen Theorie der Koagulationskinetik kolloider Lösungen, J. Phys. Chem., 92, 129, 1917.
    • (1917) J. Phys. Chem , vol.92 , pp. 129
    • Smoluchowski, V.M.1
  • 35
    • 85057252990 scopus 로고
    • The role of mobility of mitochondrial inner membrane components
    • Frangopol, A. I. Cuza University Press, Jasi, Romania
    • Lenaz, G., The role of mobility of mitochondrial inner membrane components, Curr Topics Biophys. (Jasi) vol. 2, Frangopol, A. I. Cuza University Press, Jasi, Romania, 1993, 52.
    • (1993) Curr Topics Biophys , vol.2 , pp. 52
    • Lenaz, G.1
  • 37
    • 0020102584 scopus 로고
    • Role of the protein outside active site on the diffusion-controlled reaction of enzyme
    • Chou, K. C. and Zhou, G. P. J., Role of the protein outside active site on the diffusion-controlled reaction of enzyme, Am. Chem. Soc., 104, 1409, 1982.
    • (1982) Am. Chem. Soc , vol.104 , pp. 1409
    • Chou, K.C.1    Zhou, G.P.J.2
  • 38
    • 0019319463 scopus 로고
    • Oxidation of cytochromes c and c2 by bacterial photosynthetic reaction centers in phospholipid vesicles. 2. Studies with negative membranes
    • Overfield, R. E. and Wright, C. A., Oxidation of cytochromes c and c2 by bacterial photosynthetic reaction centers in phospholipid vesicles. 2. Studies with negative membranes, Biochemistry, 19, 3328, 1980.
    • (1980) Biochemistry , vol.19 , pp. 3328
    • Overfield, R.E.1    Wright, C.A.2
  • 39
    • 0023340216 scopus 로고
    • A method for estimating lateral diffusion coefficients in membranes from steady-state fluorescence quenching studies
    • Blackwell, M. F., Gounaris, K., Zara, S. J., and Barber, J., A method for estimating lateral diffusion coefficients in membranes from steady-state fluorescence quenching studies, Biophys. J., 51, 735, 1987.
    • (1987) Biophys. J , vol.51 , pp. 735
    • Blackwell, M.F.1    Gounaris, K.2    Zara, S.J.3    Barber, J.4
  • 40
    • 0021484926 scopus 로고
    • Kinetics of carbonic anhydrase catalysis in solvents of increased viscosity: A partially diffusion-controlled reaction
    • Hasinoff, B. B., Kinetics of carbonic anhydrase catalysis in solvents of increased viscosity: a partially diffusion-controlled reaction, Arch. Biochem. Biophys., 283, 676, 1984.
    • (1984) Arch. Biochem. Biophys , vol.283 , pp. 676
    • Hasinoff, B.B.1
  • 41
    • 0018401188 scopus 로고
    • The role of lipids in the structure and function of membranes
    • Lenaz, G., The role of lipids in the structure and function of membranes, Subcell. Biochem., 6, 233, 1979.
    • (1979) Subcell. Biochem , vol.6 , pp. 233
    • Lenaz, G.1
  • 43
    • 0346277702 scopus 로고
    • Florkin & Stotz, Elsevier, Amsterdam
    • Green, D. E., Comprehensive Biochemistry, Florkin & Stotz, Elsevier, Amsterdam, 1966, 309.
    • (1966) Comprehensive Biochemistry , pp. 309
    • Green, D.E.1
  • 44
    • 0020494216 scopus 로고
    • Arrangement of proteins in the mitochondrial inner membrane
    • Capaldi, R. A., Arrangement of proteins in the mitochondrial inner membrane, Biochim. Biophys. Acta, 694, 291, 1982.
    • (1982) Biochim. Biophys. Acta , vol.694 , pp. 291
    • Capaldi, R.A.1
  • 46
    • 0023680684 scopus 로고
    • The role of mobility of redox components in the inner mitochondrial membrane
    • Lenaz, G., The role of mobility of redox components in the inner mitochondrial membrane, J. Membr. Biol, 104, 193, 1988.
    • (1988) J. Membr. Biol , vol.104 , pp. 193
    • Lenaz, G.1
  • 47
    • 0021449779 scopus 로고
    • Lateral diffusion, collision and efficiency of oxidation-reduction components in mitochondrial electron transport
    • Hackenbrock, C. R., Gupte, S., Wu, E. S., and Jacobson, K., Lateral diffusion, collision and efficiency of oxidation-reduction components in mitochondrial electron transport, Biochem. Soc. Trans., 12, 402, 1984.
    • (1984) Biochem. Soc. Trans , vol.12 , pp. 402
    • Hackenbrock, C.R.1    Gupte, S.2    Wu, E.S.3    Jacobson, K.4
  • 48
    • 0021815336 scopus 로고
    • Mobility in the mitochondrial electron transport chain
    • Hochman, H. J., Ferguson-Miller, S., and Schindler, M., Mobility in the mitochondrial electron transport chain, Biochemistry, 24, 2509, 1985.
    • (1985) Biochemistry , vol.24 , pp. 2509
    • Hochman, H.J.1    Ferguson-Miller, S.2    Schindler, M.3
  • 49
    • 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, S. H., Yu, L., and Yu, C. A., 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, 1986.
    • (1986) Biochemistry , vol.25 , pp. 7675
    • Gwak, S.H.1    Yu, L.2    Yu, C.A.3
  • 50
    • 0019770975 scopus 로고
    • Rate of lateral diffusion of intramembrane particles: Measurement by electrophoretic displacement and rerandomization
    • Sowers, A. E. and Hackenbrock, C. R., Rate of lateral diffusion of intramembrane particles: measurement by electrophoretic displacement and rerandomization, Proc. Natl. Acad. Sci., USA, 78, 6246, 1981.
    • (1981) Proc. Natl. Acad. Sci., USA , vol.78 , pp. 6246
    • Sowers, A.E.1    Hackenbrock, C.R.2
  • 51
    • 0021430791 scopus 로고
    • Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidation-reduction components
    • Gupte, S., Wu, E. S., Hoechli, L., Hoechli, M., Jacobson, K., Sowers, A. E., and Hackenbrock, C. R., Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidation-reduction components, Proc. Natl. Acad. Sci., USA, 81, 2606, 1984.
    • (1984) Proc. Natl. Acad. Sci , vol.81 , pp. 2606
    • Gupte, S.1    Wu, E.S.2    Hoechli, L.3    Hoechli, M.4    Jacobson, K.5    Sowers, A.E.6    Hackenbrock, C.R.7
  • 52
    • 0020105638 scopus 로고
    • Extraction of membrane microviscosity from translational and rotational diffusion coefficients
    • Hughes, B. D., Pailthorpe, B. A., White, L. R., and Sawyer, W. H., Extraction of membrane microviscosity from translational and rotational diffusion coefficients, Biophys. J., 37, 673, 1982.
    • (1982) Biophys. J , vol.37 , pp. 673
    • Hughes, B.D.1    Pailthorpe, B.A.2    White, L.R.3    Sawyer, W.H.4
  • 53
    • 0026716564 scopus 로고
    • On coenzyme q orientation in membranes: A linear dichroism study of ubiquinones in a model bilayer
    • Samori, B., Lenaz, G., Battino, M., Marconi, G., and Domini, I., On coenzyme Q orientation in membranes: a linear dichroism study of ubiquinones in a model bilayer, J. Membr. Biol., 128, 193, 1992.
    • (1992) J. Membr. Biol , vol.128 , pp. 193
    • Samori, B.1    Lenaz, G.2    Battino, M.3    Marconi, G.4    Domini, I.5
  • 55
    • 0018697544 scopus 로고
    • Vectorial redox reactions of physiological quinones. II. A study of transient semiquinone formation
    • Futami, A., Hurt, E., and Hauska, G., Vectorial redox reactions of physiological quinones. II. A study of transient semiquinone formation, Biochim. Biophys. Acta, 547, 583, 1979.
    • (1979) Biochim. Biophys. Acta , vol.547 , pp. 583
    • Futami, A.1    Hurt, E.2    Hauska, G.3
  • 57
    • 0021735199 scopus 로고
    • On the localization of ubiquinone in phosphatidylcholine bilayers
    • Stidham, M. A., McIntosh, T. J., and Siedow, J. N., On the localization of ubiquinone in phosphatidylcholine bilayers, Biochim. Biophys. Acta, 767, 423, 1984.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 423
    • Stidham, M.A.1    McIntosh, T.J.2    Siedow, J.N.3
  • 58
    • 0032502940 scopus 로고    scopus 로고
    • High diffusion coefficients for coenzyme q homologs may be due to a folded conformation
    • Di Bernardo, S., Fato, R., Casadio, R., Fariselli, P., and Lenaz, G., High diffusion coefficients for Coenzyme Q homologs may be due to a folded conformation, FEBS Lett., 426, 77, 1998.
    • (1998) FEBS Lett , vol.426 , pp. 77
    • Di Bernardo, S.1    Fato, R.2    Casadio, R.3    Fariselli, P.4    Lenaz, G.5
  • 60
    • 0031067782 scopus 로고    scopus 로고
    • Epr, endor and triple resonance and mo studies on ubiquinones (Q-n): Comparison of radical anions and cations of coenzymes q-10 and q-6 with the model compounds q-2 and q-0
    • Joela, H., Kasa, S., Lehtovuori, P, and Bech, M., EPR, ENDOR and TRIPLE resonance and MO studies on ubiquinones (Q-n): comparison of radical anions and cations of coenzymes Q-10 and Q-6 with the model compounds Q-2 and Q-0, Acta Chem. Scand., 51, 233, 1997.
    • (1997) Acta Chem. Scand , vol.51 , pp. 233
    • Joela, H.1    Kasa, S.2    Lehtovuori, P.3    Bech, M.4
  • 61
    • 0033082337 scopus 로고    scopus 로고
    • The interaction of coenzyme q with phosphatidylethanolamine membranes
    • Gomez-Fernandez, J. C., Llamas, M. A., and Aranda, F. J., The interaction of coenzyme Q with phosphatidylethanolamine membranes, Eur J. Biochem., 259, 739, 1999.
    • (1999) Eur J. Biochem , vol.259 , pp. 739
    • Gomez-Fernandez, J.C.1    Llamas, M.A.2    Aranda, F.J.3
  • 62
    • 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., and 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, 1986.
    • (1986) Biochemistry , vol.25 , pp. 3378
    • Fato, R.1    Battino, M.2    Degli Esposti, M.3    Parenti Castelli, G.4    Lenaz, G.5
  • 63
    • 0024594990 scopus 로고
    • Synthesis, location, and lateral mobility of fluorescently labeled ubiquinone 10 in mitochondrial and artificial membranes
    • Rajarathnam, K., Hochman, J., Schindler, M., and Ferguson-Miller, S., Synthesis, location, and lateral mobility of fluorescently labeled ubiquinone 10 in mitochondrial and artificial membranes, Biochemistry, 28, 3168, 1989.
    • (1989) Biochemistry , vol.28 , pp. 3168
    • Rajarathnam, K.1    Hochman, J.2    Schindler, M.3    Ferguson-Miller, S.4
  • 64
    • 0023808978 scopus 로고
    • The multicollisional, obstructed, long-range diffusional nature of mitochondrial electron transport
    • Chazotte, B. and Hackenbrock, C. R., The multicollisional, obstructed, long-range diffusional nature of mitochondrial electron transport, J. Biol. Chem., 263, 14359, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 14359
    • Chazotte, B.1    Hackenbrock, C.R.2
  • 65
    • 0026050568 scopus 로고
    • Lateral diffusion of redox components in the mitochondrial inner membrane is unaffected by inner membrane folding and matrix density
    • Chazotte, B. and Hackenbrock, C. R., Lateral diffusion of redox components in the mitochondrial inner membrane is unaffected by inner membrane folding and matrix density, J. Biol. Chem., 266, 5973, 1991.
    • (1991) J. Biol. Chem , vol.266 , pp. 5973
    • Chazotte, B.1    Hackenbrock, C.R.2
  • 67
    • 0027191299 scopus 로고
    • Steady-state kinetics of ubiquinol-cytochrome c reductase in saccharomyces cerevisiae mitochondria: Effects of fluidity changes obtained by different growth temperatures
    • Cavazzoni, M., Svobodova, J., De Santis, A., Fato, R., and Lenaz, G., Steady-state kinetics of ubiquinol-cytochrome c reductase in Saccharomyces cerevisiae mitochondria: effects of fluidity changes obtained by different growth temperatures, Arch. Biochem. Biophys., 303, 246, 1993.
    • (1993) Arch. Biochem. Biophys , vol.303 , pp. 246
    • Cavazzoni, M.1    Svobodova, J.2    De Santis, A.3    Fato, R.4    Lenaz, G.5
  • 68
    • 0031920484 scopus 로고    scopus 로고
    • Electrochemical measurement of lateral diffusion coefficients of ubiquinones and plastoquinone of various isoprenoid chain lengths incorporated in model bilayers
    • Marchal, D., Boireau, W., Laval, J. M., Moiroux, J., and Bourdillon, C., Electrochemical measurement of lateral diffusion coefficients of ubiquinones and plastoquinone of various isoprenoid chain lengths incorporated in model bilayers, Biophys, J., 74, 1937, 1998.
    • (1998) Biophys, J , vol.74 , pp. 1937
    • Marchal, D.1    Boireau, W.2    Laval, J.M.3    Moiroux, J.4    Bourdillon, C.5
  • 69
    • 0028387998 scopus 로고
    • Electrochemical measurements of the lateral diffusion of electroactive amphiphiles in supported phospholipid monolayers
    • Torchut, E., Laval, J. M., Bourdillon, C., and Majda, M., Electrochemical measurements of the lateral diffusion of electroactive amphiphiles in supported phospholipid monolayers., Biophys. J., 66, 753, 1994.
    • (1994) Biophys. J , vol.66 , pp. 753
    • Torchut, E.1    Laval, J.M.2    Bourdillon, C.3    Majda, M.4
  • 70
    • 0025188810 scopus 로고
    • Effect of integral membrane proteins on the lateral mobility of plastoquinone in phosphatidylcholine proteoliposomes
    • Blackwell, M. F. and Whitmarsh, T., Effect of integral membrane proteins on the lateral mobility of plastoquinone in phosphatidylcholine proteoliposomes, Biophys. J., 58, 1259, 1990.
    • (1990) Biophys. J , vol.58 , pp. 1259
    • Blackwell, M.F.1    Whitmarsh, T.2
  • 71
    • 0343254011 scopus 로고
    • Lateral diffusion of lipids and proteins in bilayer membranes
    • Vaz, W. L. C., Goodsaid-Zalbuondo, F., and Jacobson, K., Lateral diffusion of lipids and proteins in bilayer membranes, FEBS Lett., 174, 199, 1984.
    • (1984) FEBS Lett , vol.174 , pp. 199
    • Vaz, W.L.C.1    Goodsaid-Zalbuondo, F.2    Jacobson, K.3
  • 72
    • 0028000886 scopus 로고
    • Comparisons of the relative effects of polyhydroxyl compounds on local versus long-range motions in the mitochondrial inner membrane. Fluorescence recovery after photobleaching, fluorescence lifetime, and fluorescence anisotropy studies
    • Chazotte B., Comparisons of the relative effects of polyhydroxyl compounds on local versus long-range motions in the mitochondrial inner membrane. Fluorescence recovery after photobleaching, fluorescence lifetime, and fluorescence anisotropy studies, Biochim. Biophys. Acta, 1194, 315, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1194 , pp. 315
    • Chazotte, B.1
  • 73
    • 0028365478 scopus 로고
    • Changes in the lipid dynamics of liposomal membranes induced by poly(Ethylene glycol): Free volume alterations revealed by inter- and intramolecular excimer-forming phospholipid analogs
    • Lehtonen, J. Y and Kinnunen, P. K., Changes in the lipid dynamics of liposomal membranes induced by poly(ethylene glycol): free volume alterations revealed by inter- and intramolecular excimer-forming phospholipid analogs, Biophys. J., 66, 1981, 1994.
    • (1994) Biophys. J , vol.66 , pp. 1981
    • Lehtonen, J.Y.1    Kinnunen, P.K.2
  • 74
    • 0027264486 scopus 로고
    • Rate-limiting step in electron transport. Osmotically sensitive diffusion of quinones through voids in the bilayer
    • Mathai, J. C., Sauna, Z. E., John, O., and Sitaramam, V, Rate-limiting step in electron transport. Osmotically sensitive diffusion of quinones through voids in the bilayer, J. Biol. Chem., 268, 15442, 1993.
    • (1993) J. Biol. Chem , vol.268 , pp. 15442
    • Mathai, J.C.1    Sauna, Z.E.2    John, O.3    Sitaramam, V.4
  • 75
    • 0015607377 scopus 로고
    • The kinetics of redox reactions of ubiquinone related to the electron transport activity of the respiratory chain
    • Kröger, A. and Klingenberg, M., The kinetics of redox reactions of ubiquinone related to the electron transport activity of the respiratory chain, Eur. J. Biochem., 34, 358, 1973.
    • (1973) Eur. J. Biochem , vol.34 , pp. 358
    • Kröger, A.1    Klingenberg, M.2
  • 76
    • 0011106782 scopus 로고
    • Lenaz, Wiley, Chichester
    • Gutman, M., Coenzyme Q, Lenaz, Wiley, Chichester, 1985, 215.
    • (1985) Coenzyme Q , pp. 215
    • Gutman, M.1
  • 77
    • 46549100769 scopus 로고
    • The kinetics of quinone pools in electron transport
    • Ragan, C. I. and Cottingham, I. R., The kinetics of quinone pools in electron transport, Biochim. Biophys. Acta, 811, 13, 1985.
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 13
    • Ragan, C.I.1    Cottingham, I.R.2
  • 78
    • 0026778904 scopus 로고
    • Saturation kinetics of coenzyme q in nadh and succinate oxidation in beef heart mitochondria
    • Estornell, E., Fato, R., Castelluccio, C., Cavazzoni, M., Parenti Castelli, G., and Lenaz, G., Saturation kinetics of Coenzyme Q in NADH and succinate oxidation in beef heart mitochondria, FEBS Lett., 311, 107, 1992.
    • (1992) FEBS Lett , vol.311 , pp. 107
    • Estornell, E.1    Fato, R.2    Castelluccio, C.3    Cavazzoni, M.4    Parenti Castelli, G.5    Lenaz, G.6
  • 81
    • 0016288208 scopus 로고
    • Studies with ubiquinone-depleted submitochondrial particles. Quantitative incorporation of small amounts of ubiquinone and its effects on the nadh and succinate oxidase activities
    • Norling, B., Glazek, E., Nelson, B. D., and Ernster, L., Studies with ubiquinone-depleted submitochondrial particles. Quantitative incorporation of small amounts of ubiquinone and its effects on the NADH and succinate oxidase activities, Eur. J. Biochem., 47, 475, 1974.
    • (1974) Eur. J. Biochem , vol.47 , pp. 475
    • Norling, B.1    Glazek, E.2    Nelson, B.D.3    Ernster, L.4
  • 82
    • 0020491098 scopus 로고
    • Lateral diffusion of ubiquinone during electron transfer in phospholipid- and ubiquinone-enriched mitochondrial membranes
    • Schneider, H., Lemasters, J. J., and Hackenbrock, C. R., Lateral diffusion of ubiquinone during electron transfer in phospholipid- and ubiquinone-enriched mitochondrial membranes, J. Biol. Chem., 257, 10789, 1982.
    • (1982) J. Biol. Chem , vol.257 , pp. 10789
    • Schneider, H.1    Lemasters, J.J.2    Hackenbrock, C.R.3
  • 83
    • 33746100806 scopus 로고
    • Kinetic studies on the pool function of ubiquinone in mitochondrial systems
    • Parenti Castelli, G., Fato, R., Battino, M., Castelluccio, C., and Lenaz, G., Kinetic studies on the pool function of ubiquinone in mitochondrial systems, Chem. Scr., 27, 161, 1987.
    • (1987) Chem. Scr , vol.27 , pp. 161
    • Parenti Castelli, G.1    Fato, R.2    Battino, M.3    Castelluccio, C.4    Lenaz, G.5
  • 84
    • 0019644226 scopus 로고
    • Spectroscopic properties of ubiquinones in model systems
    • Degli Esposti, M., Ferri, E., and Lenaz, G., Spectroscopic properties of ubiquinones in model systems, Ital. J. Biochem., 30, 437, 1981.
    • (1981) Ital. J. Biochem , vol.30 , pp. 437
    • Degli Esposti, M.1    Ferri, E.2    Lenaz, G.3
  • 85
    • 0022836506 scopus 로고
    • A difference infrared-spectroscopic study of the interaction of ubiquinone-10 with phospholipid bilayers
    • Ondarroa, M. and Quinn, P. J., A difference infrared-spectroscopic study of the interaction of ubiquinone-10 with phospholipid bilayers, Biochem. J., 240, 325, 1986.
    • (1986) Biochem. J , vol.240 , pp. 325
    • Ondarroa, M.1    Quinn, P.J.2
  • 86
    • 0021525918 scopus 로고
    • Novel isolation of ubiquinone-binding proteins located in different sites of beef heart mitochondrial respiratory chain
    • Suzuki, H. and Ozawa, T., Novel isolation of ubiquinone-binding proteins located in different sites of beef heart mitochondrial respiratory chain, Biochem. Int., 9, 563, 1984.
    • (1984) Biochem. Int , vol.9 , pp. 563
    • Suzuki, H.1    Ozawa, T.2
  • 87
    • 84936208684 scopus 로고
    • Comparative study of quinone binding proteins in mitochondrial cytochrome b-c1 complex and chloroplast cytochrome b6-f complex
    • Lenaz, Barnabei, Rabbi, Battino, Taylor and Francis, London
    • 6-f complex, in Highlights in Ubiquinone Research, Lenaz, Barnabei, Rabbi, Battino, Taylor and Francis, London, 1990, 46.
    • (1990) Highlights in Ubiquinone Research , pp. 46
    • Yu, C.A.1    Usui, S.2    Li, L.B.3    Yu, L.4
  • 88
    • 0002856431 scopus 로고
    • Pathways of electrons and protons through the cytochrome bc1 complex of the mitochondrial respiratory chain
    • Wiley, Chichester
    • 1Complex of the mitochondrial respiratory chain, Coenzyme Q, Lenaz, Wiley, Chichester, 1985, 365.
    • (1985) Coenzyme , pp. 365
    • Berry, E.A.1    Trumpower, B.L.2
  • 89
    • 0031033436 scopus 로고    scopus 로고
    • Proton-translocation by membrane-bound nadh: Ubiquinone-oxidoreductase (complex i) through redox-gated ligand conduction
    • Brandt, U., Proton-translocation by membrane-bound NADH: ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction, Biochim. Biophys. Acta, 1318, 79, 1997.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 79
    • Brandt, U.1
  • 90
    • 0023852761 scopus 로고
    • A simple method for determination of the kinetic constants of membrane enzymes utilizing hydrophobic substrates: Ubiquinol cytochrome c reductase
    • Fato, R., Castelluccio, C., Palmer, G., and Lenaz, G., A simple method for determination of the kinetic constants of membrane enzymes utilizing hydrophobic substrates: ubiquinol cytochrome c reductase, Biochim. Biophys. Acta, 932, 216, 1988.
    • (1988) Biochim. Biophys. Acta , vol.932 , pp. 216
    • Fato, R.1    Castelluccio, C.2    Palmer, G.3    Lenaz, G.4
  • 91
    • 0019317602 scopus 로고
    • Ubiquinol-cytochrome c reductase (Ec 1.10.2.2). Isolation in triton x-100 by hydroxyapatite and gel chromatography. Structural and functional properties
    • Engel, W. D., Schagger, H., and Van Jagow, G., Ubiquinol-cytochrome c reductase (EC 1.10.2.2). Isolation in triton X-100 by hydroxyapatite and gel chromatography. Structural and functional properties, Biochim. Biophys. Acta, 592, 211, 1980.
    • (1980) Biochim. Biophys. Acta , vol.592 , pp. 211
    • Engel, W.D.1    Schagger, H.2    Van Jagow, G.3
  • 92
    • 0024514220 scopus 로고
    • Modelling of chemical reactions catalysed by membrane-bound enzymes. Determination and significance of the kinetic constants
    • Heirwegh, K. P. M., Meuwisson, J. A. T. P., Van den Steen, P., and De Smedt, H., Modelling of chemical reactions catalysed by membrane-bound enzymes. Determination and significance of the kinetic constants, Biochim. Biophys. Acta, 995, 151, 1989.
    • (1989) Biochim. Biophys. Acta , vol.995 , pp. 151
    • Heirwegh, K.P.M.1    Meuwisson, J.A.T.P.2    Van Den Steen, P.3    De Smedt, H.4
  • 93
    • 0023649029 scopus 로고
    • The kinetics of the aerobic oxidation of ferrocytochrome c by cytochrome c oxidase in solvents of increased viscosity are partially diffusion controlled
    • Hasinoff, B. B. and Davey, J. P., The kinetics of the aerobic oxidation of ferrocytochrome c by cytochrome c oxidase in solvents of increased viscosity are partially diffusion controlled, Biochim. Biophys. Acta, 892, 1, 1987.
    • (1987) Biochim. Biophys. Acta , vol.892 , pp. 1
    • Hasinoff, B.B.1    Davey, J.P.2
  • 94
    • 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., and Lenaz, G., Steady-state kinetics of ubiquinol-cytochrome c reductase in bovine heart submitochondrial particles: diffusional effects, Biochem. J., 290, 225, 1993.
    • (1993) Biochem. J , vol.290 , pp. 225
    • Fato, R.1    Cavazzoni, M.2    Castelluccio, C.3    Parenti Castelli, G.4    Palmer, G.5    Degli Esposti, M.6    Lenaz, G.7
  • 95
    • 0025935594 scopus 로고
    • The kinetic mechanism of ubiquinol: Cytochrome c reductase at steady-state
    • Degli Esposti, M. and Lenaz, G., The kinetic mechanism of ubiquinol: cytochrome c reductase at steady-state, Arch. Biochem. Biophys., 289, 303, 1991.
    • (1991) Arch. Biochem. Biophys , vol.289 , pp. 303
    • Degli Esposti, M.1    Lenaz, G.2
  • 96
    • 0022796982 scopus 로고
    • Reaction center and uqh2: Cyt c2 oxidoreductase act as independent enzymes in
    • Crofts, A. R., Reaction center and UQH2: cyt c2 oxidoreductase act as independent enzymes in Rps. Sphaeroides, J. Bioenerg. Biomembr., 18, 437, 1986.
    • (1986) Rps. Sphaeroides, J. Bioenerg. Biomembr , vol.18 , pp. 437
    • Crofts, A.R.1
  • 98
    • 44049113644 scopus 로고
    • Kinetic aspects of the interaction of cytochrome c with ubiquinol cytochrome c reductase in beef heart submitochondrial particles
    • Fato, R., Cavazzoni, M., Castelluccio C., Baracca, A., Parenti Castelli, G., and Lenaz, G., Kinetic aspects of the interaction of cytochrome c with ubiquinol cytochrome c reductase in beef heart submitochondrial particles, Bioelectrochem. Bioenerg., 28, 177, 1992.
    • (1992) Bioelectrochem. Bioenerg , vol.28 , pp. 177
    • Fato, R.1    Cavazzoni, M.2    Castelluccio, C.3    Baracca, A.4    Parenti Castelli, G.5    Lenaz, G.6
  • 99
    • 0017818725 scopus 로고
    • Diffusional increase and decrease in half-maximal-activity substrate concentrations with two-substrate enzymic reactions
    • Engasser, J. M. and Hisland, P., Diffusional increase and decrease in half-maximal-activity substrate concentrations with two-substrate enzymic reactions, Biochem. J., 173, 341, 1978.
    • (1978) Biochem. J , vol.173 , pp. 341
    • Engasser, J.M.1    Hisland, P.2
  • 100
    • 0021119024 scopus 로고
    • Lactate dehydrogenase associated with the mitochondrial fraction and with a mitochondrial inhibitor i. Enzyme binding to the mitochondrial fraction
    • Lluis, C., Lactate dehydrogenase associated with the mitochondrial fraction and with a mitochondrial inhibitor I. Enzyme binding to the mitochondrial fraction, Int. J. Biochem., 16, 997, 1984.
    • (1984) Int. J. Biochem , vol.16 , pp. 997
    • Lluis, C.1
  • 101
    • 0017268663 scopus 로고
    • Kinetic behavior of immobilized enzyme systems
    • Goldstein, L., Kinetic behavior of immobilized enzyme systems, Methods Enzymol., 44, 397, 1976.
    • (1976) Methods Enzymol , vol.44 , pp. 397
    • Goldstein, L.1
  • 102
    • 0016264702 scopus 로고
    • Two temperature-induced changes in mitochondrial membranes detected by spin labelling and enzyme kinetics
    • Raison, J. K. and McMurchie, E. J., Two temperature-induced changes in mitochondrial membranes detected by spin labelling and enzyme kinetics, Biochim. Biophys. Acta, 363, 135, 1974.
    • (1974) Biochim. Biophys. Acta , vol.363 , pp. 135
    • Raison, J.K.1    McMurchie, E.J.2
  • 103
    • 0011886463 scopus 로고
    • Membrane fluidity: Molecular basis and physiological significance
    • Benga, CRC Press, Boca Raton, FL
    • Lenaz, G. and Parenti Castelli, G., Membrane fluidity: molecular basis and physiological significance, in Structure and Properties ofCell Membranes, vol. 1, Benga, CRC Press, Boca Raton, FL, 1985, 93.
    • (1985) Structure and Properties Ofcell Membranes , vol.1 , pp. 93
    • Lenaz, G.1    Parenti Castelli, G.2
  • 104
    • 0025794314 scopus 로고
    • The mobility of a fluorescent ubiquinone in model lipid membranes. Relevance to mitochondrial electron transport
    • Chazotte B., Wu E. S., and Hackenbrock C. R., The mobility of a fluorescent ubiquinone in model lipid membranes. Relevance to mitochondrial electron transport, Biochim. Biophys. Acta, 1058, 400, 1991.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 400
    • Chazotte, B.1    Wu, E.S.2    Hackenbrock, C.R.3
  • 105
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle, P. L., Cholesterol and the cell membrane, Biochim. Biophys. Acta, 822, 267, 1985.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 267
    • Yeagle, P.L.1
  • 106
    • 0029914228 scopus 로고    scopus 로고
    • Steady-state kinetics of the reduction of coenzyme q analogs by complex i in bovine heart mitochondria and submitochondrial particles
    • Fato, R., Estornell, E., Di Bernardo, S., Pallotti, F., Parenti Castelli, G., and Lenaz, G., Steady-state kinetics of the reduction of Coenzyme Q analogs by Complex I in bovine heart mitochondria and submitochondrial particles, Biochemistry, 35, 2705, 1996.
    • (1996) Biochemistry , vol.35 , pp. 2705
    • Fato, R.1    Estornell, E.2    Di Bernardo, S.3    Pallotti, F.4    Parenti Castelli, G.5    Lenaz, G.6
  • 107
    • 0018987756 scopus 로고
    • Modulation of membrane protein lateral mobility by polyphosphates and polyamines
    • Schindler, M., Koppel, D. E., and Sheetz, M. P., Modulation of membrane protein lateral mobility by polyphosphates and polyamines, Proc. Natl. Acad. Sci., USA, 77, 1457, 1980.
    • (1980) Proc. Natl. Acad. Sci , vol.77 , pp. 1457
    • Schindler, M.1    Koppel, D.E.2    Sheetz, M.P.3
  • 108
    • 0019331569 scopus 로고
    • Comparative lateral diffusion of fluorescent lipid analogues in phospholipid multibilayers
    • Derzko, Z. and Jacobson, K., Comparative lateral diffusion of fluorescent lipid analogues in phospholipid multibilayers, Biochemistry, 19, 6055, 1980.
    • (1980) Biochemistry , vol.19 , pp. 6055
    • Derzko, Z.1    Jacobson, K.2
  • 109
    • 0023948895 scopus 로고
    • The role of cytochrome c diffusion in mitochondrial electron transport
    • Gupte, S. S. and Hackenbrock, C. R., The role of cytochrome c diffusion in mitochondrial electron transport, J. Biol. Chem, 263, 5248, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 5248
    • Gupte, S.S.1    Hackenbrock, C.R.2
  • 110
    • 84936493837 scopus 로고
    • Effect of phospholipid enrichment on the turnover of electron transfer in mitochondrial membranes and isolated nadh cytochrome c reductase
    • Parenti Castelli, G., Fato, R., and Lenaz, G., Effect of phospholipid enrichment on the turnover of electron transfer in mitochondrial membranes and isolated NADH cytochrome c reductase, Life Sci. Adv., 7, 219, 1988.
    • (1988) Life Sci. Adv , vol.7 , pp. 219
    • Parenti Castelli, G.1    Fato, R.2    Lenaz, G.3
  • 111
    • 0021264942 scopus 로고
    • 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, C. and J. 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, 1984.
    • (1984) Bioenerg. Biomembr , vol.16 , pp. 115
    • Stoner, C.1    Steady-State, J.2
  • 112
    • 0342872005 scopus 로고    scopus 로고
    • Coenzyme q homologs and vitamin e in synaptic and non-synaptic occipital cerebral cortex mitochondria in the aging rat
    • Littarru, G., Alleva, R., Battino, M., and Folkers, K., Coenzyme Q homologs and vitamin E in synaptic and non-synaptic occipital cerebral cortex mitochondria in the aging rat, Mol. Aspects Med., 18 (suppl.), S279, 1997.
    • (1997) Mol. Aspects Med , vol.18 , pp. S279
    • Littarru, G.1    Alleva, R.2    Battino, M.3    Folkers, K.4


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