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Volumn 47, Issue , 2010, Pages 53-67

Mitochondrial proton and electron leaks

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA;

EID: 79551610255     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/BSE0470053     Document Type: Article
Times cited : (598)

References (51)
  • 1
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell, P. (1961) Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191, 144-148
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 2
    • 0025359843 scopus 로고
    • Non-ohmic proton conductance of the mitochondrial inner membrane in hepatocytes
    • Nobes, C.D., Brown, G.C., Olive, P.N. and Brand, M.D. (1990) Non-ohmic proton conductance of the mitochondrial inner membrane in hepatocytes. J. Biol. Chem. 265, 12903-12909
    • (1990) J. Biol. Chem , vol.265 , pp. 12903-12909
    • Nobes, C.D.1    Brown, G.C.2    Olive, P.N.3    Brand, M.D.4
  • 3
    • 0037726805 scopus 로고    scopus 로고
    • Intrinsic and extrinsic uncoupling of oxidative phosphorylation
    • Kadenbach, B. (2003) Intrinsic and extrinsic uncoupling of oxidative phosphorylation. Biochim. Biophys. Acta 1604, 77-94
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 77-94
    • Kadenbach, B.1
  • 4
    • 0025854301 scopus 로고
    • Effect of protonmotive force on the relative proton stoichiometries of the mitochondrial proton pumps
    • Hafner, R.P. and Brand, M.D. (1991) Effect of protonmotive force on the relative proton stoichiometries of the mitochondrial proton pumps. Biochem. J. 275, 75-80
    • (1991) Biochem. J. , vol.275 , pp. 75-80
    • Hafner, R.P.1    Brand, M.D.2
  • 5
    • 0024422115 scopus 로고
    • Slip and leak in mitochondrial oxidative phosphorylation
    • Murphy, M.P. (1989) Slip and leak in mitochondrial oxidative phosphorylation. Biochim. Biophys. Acta 977, 123-141
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 123-141
    • Murphy, M.P.1
  • 6
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M.P. (2009) How mitochondria produce reactive oxygen species. Biochem. J. 417, 1-13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 7
    • 0030809576 scopus 로고    scopus 로고
    • Reactive oxygen species, mitochondria, apoptosis and aging
    • Papa, S. and Skulachev, V.P. (1997) Reactive oxygen species, mitochondria, apoptosis and aging. Mol. Cell. Biochem. 174, 305-319
    • (1997) Mol. Cell. Biochem , vol.174 , pp. 305-319
    • Papa, S.1    Skulachev, V.P.2
  • 10
    • 70349971955 scopus 로고    scopus 로고
    • Uncoupling protein-1 (UCP1) contributes to the basal proton conductance of brown adipose tissue mitochondria
    • Parker, N., Crichton, P.G., Vidal-Puig, A.J. and Brand, M.D. (2009) Uncoupling protein-1 (UCP1) contributes to the basal proton conductance of brown adipose tissue mitochondria. J. Bioenerg. Biomembr. 41, 335-342
    • (2009) J. Bioenerg. Biomembr , vol.41 , pp. 335-342
    • Parker, N.1    Crichton, P.G.2    Vidal-Puig, A.J.3    Brand, M.D.4
  • 11
  • 12
    • 0029976895 scopus 로고    scopus 로고
    • Contribution of mitochondrial proton leak to skeletal muscle respiration and to standard metabolic rate
    • Rolfe, D.F.S. and Brand, M.D. (1996) Contribution of mitochondrial proton leak to skeletal muscle respiration and to standard metabolic rate. Am. J. Physiol. 271, C1380-C1389
    • (1996) Am. J. Physiol , vol.271
    • Rolfe, D.F.S.1    Brand, M.D.2
  • 13
    • 33847752716 scopus 로고    scopus 로고
    • Mitochondrial function, fibre types and ageing: New insights from human muscle in vivo
    • Conley, K.E., Amara, C.E., Jubrias, S.A. and Marcinek, D.J. (2007) Mitochondrial function, fibre types and ageing: new insights from human muscle in vivo. Exp. Physiol. 92, 333-339
    • (2007) Exp. Physiol , vol.92 , pp. 333-339
    • Conley, K.E.1    Amara, C.E.2    Jubrias, S.A.3    Marcinek, D.J.4
  • 14
    • 65449174289 scopus 로고    scopus 로고
    • Measuring mitochondrial bioenergetics in INS-1E insulinoma cells
    • Affourtit, C. and Brand, M.D. (2009) Measuring mitochondrial bioenergetics in INS-1E insulinoma cells. Methods Enzymol. 457, 405-424
    • (2009) Methods Enzymol , vol.457 , pp. 405-424
    • Affourtit, C.1    Brand, M.D.2
  • 15
    • 48249083981 scopus 로고    scopus 로고
    • Stimulation of mitochondrial proton conductance by hydroxynonenal requires a high membrane potential
    • Parker, N., Vidal-Puig, A. and Brand, M.D. (2008) Stimulation of mitochondrial proton conductance by hydroxynonenal requires a high membrane potential. Biosci. Rep. 28, 83-88
    • (2008) Biosci. Rep , vol.28 , pp. 83-88
    • Parker, N.1    Vidal-Puig, A.2    Brand, M.D.3
  • 16
    • 0347989317 scopus 로고    scopus 로고
    • Brown adipose tissue: Function and physiological significance
    • Cannon, B. and Nedergaard, J. (2004) Brown adipose tissue: function and physiological significance. Physiol. Rev. 84, 277-359
    • (2004) Physiol. Rev , vol.84 , pp. 277-359
    • Cannon, B.1    Nedergaard, J.2
  • 17
    • 0022327490 scopus 로고
    • The reconstituted isolated uncoupling protein is a membrane potential driven H+ translocator
    • Klingenberg, M. and Winkler, E. (1985) The reconstituted isolated uncoupling protein is a membrane potential driven H+ translocator. EMBO J. 4, 3087-3092
    • (1985) EMBO J. , vol.4 , pp. 3087-3092
    • Klingenberg, M.1    Winkler, E.2
  • 18
    • 0030039607 scopus 로고    scopus 로고
    • On the mechanism of fatty acid-induced proton transport by mitochondrial uncoupling protein
    • Garlid, K.D., Orosz, D.E., Modriansky, M., Vassanelli, S. and Jezek, P. (1996) On the mechanism of fatty acid-induced proton transport by mitochondrial uncoupling protein. J. Biol. Chem. 271, 2615-2620
    • (1996) J. Biol. Chem , vol.271 , pp. 2615-2620
    • Garlid, K.D.1    Orosz, D.E.2    Modriansky, M.3    Vassanelli, S.4    Jezek, P.5
  • 19
    • 1042286448 scopus 로고    scopus 로고
    • Alkylsulfonates activate the uncoupling protein UCP1: Implications for the transport mechanism
    • Rial, E., Aquirregoitia, E., Jimenez-Jimenez, J. and Ledesma, A. (2004) Alkylsulfonates activate the uncoupling protein UCP1: implications for the transport mechanism. Biochim. Biophys. Acta 1608, 122-130
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 122-130
    • Rial, E.1    Aquirregoitia, E.2    Jimenez-Jimenez, J.3    Ledesma, A.4
  • 20
    • 4644295401 scopus 로고    scopus 로고
    • Native UCP1 displays simple competitive kinetics between the regulators purine nucleotides and fatty acids
    • Shabalina, I.G., Jacobsson, A., Cannon, B. and Nedergaard, J. (2004) Native UCP1 displays simple competitive kinetics between the regulators purine nucleotides and fatty acids. J. Biol. Chem. 279, 38236-38248
    • (2004) J. Biol. Chem , vol.279 , pp. 38236-38248
    • Shabalina, I.G.1    Jacobsson, A.2    Cannon, B.3    Nedergaard, J.4
  • 23
    • 25144489463 scopus 로고    scopus 로고
    • Uncoupling protein 1 in fish uncovers an ancient evolutionary history of mammalian nonshivering thermogenesis
    • Jastroch, M., Wuertz, S., Kloas, W. and Klingenspor, M. (2005) Uncoupling protein 1 in fish uncovers an ancient evolutionary history of mammalian nonshivering thermogenesis. Physiol. Genomics 22, 150-156
    • (2005) Physiol. Genomics , vol.22 , pp. 150-156
    • Jastroch, M.1    Wuertz, S.2    Kloas, W.3    Klingenspor, M.4
  • 25
    • 33748969187 scopus 로고    scopus 로고
    • Participation of ATP/ADP antiporter in oleate- and oleate hydroperoxide-induced uncoupling suppressed by GDP and carboxyatractylate
    • Khailova, L.S., Pridhodko, E.A., Dedukhove, V.I., Mokhova, E.N., Popov, V.N. and Skulachev, V.P. (2006) Participation of ATP/ADP antiporter in oleate- and oleate hydroperoxide-induced uncoupling suppressed by GDP and carboxyatractylate. Biochim. Biophys. Acta 1757, 1324-1329
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1324-1329
    • Khailova, L.S.1    Pridhodko, E.A.2    Dedukhove, V.I.3    Mokhova, E.N.4    Popov, V.N.5    Skulachev, V.P.6
  • 26
    • 54449089267 scopus 로고    scopus 로고
    • Essential role for uncoupling protein-3 in mitochondrial adaptation to fasting but not in fatty acid oxidation or fatty acid anion export
    • Seifert, E.L., Bezaire, V., Estey, C. and Harper, M.E. (2008) Essential role for uncoupling protein-3 in mitochondrial adaptation to fasting but not in fatty acid oxidation or fatty acid anion export. J. Biol. Chem. 283, 25124-25131
    • (2008) J. Biol. Chem , vol.283 , pp. 25124-25131
    • Seifert, E.L.1    Bezaire, V.2    Estey, C.3    Harper, M.E.4
  • 27
    • 56649103828 scopus 로고    scopus 로고
    • The mechanism of transport by mitochondrial carriers based on analysis of symmetry
    • Robinson, A.J., Overy, C. and Kunji, E.R. (2008) The mechanism of transport by mitochondrial carriers based on analysis of symmetry. Proc. Natl. Acad. Sci. U.S.A. 105, 17766-17771
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 17766-17771
    • Robinson, A.J.1    Overy, C.2    Kunji, E.R.3
  • 28
    • 0025154843 scopus 로고
    • New substrates and competitive inhibitors of the Cl- translocating pathway of the uncoupling protein of brown adipose tissue mitochondria
    • Jezek, P. and Garlid, K.D. (1990) New substrates and competitive inhibitors of the Cl- translocating pathway of the uncoupling protein of brown adipose tissue mitochondria. J. Biol. Chem. 265, 19303-19311
    • (1990) J. Biol. Chem , vol.265 , pp. 19303-19311
    • Jezek, P.1    Garlid, K.D.2
  • 30
    • 33846188870 scopus 로고    scopus 로고
    • Characteristics of α-glycerophosphate-evoked H2O2 generation in brain mitochondria
    • Tretter, L., Takacs, K., Hegedus, V. and Adam-Vizi, V. (2007) Characteristics of α-glycerophosphate-evoked H2O2 generation in brain mitochondria. J. Neurochem. 100, 650-663
    • (2007) J. Neurochem , vol.100 , pp. 650-663
    • Tretter, L.1    Takacs, K.2    Hegedus, V.3    Adam-Vizi, V.4
  • 31
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St Pierre, J., Buckingham, J.A., Roebuck, S.J. and Brand, M.D. (2002) Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277, 44784-44790
    • (2002) J. Biol. Chem , vol.277 , pp. 44784-44790
    • St Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 32
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH: Ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • Kussmaul, L. and Hirst, J. (2006) The mechanism of superoxide production by NADH: ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc. Natl. Acad. Sci. U.S.A. 103, 7607-7612
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 33
    • 53849099653 scopus 로고    scopus 로고
    • The production of reactive oxygen species by complex i
    • Hirst, J., King, M.S. and Pryde, K.R. (2008) The production of reactive oxygen species by complex I. Biochem. Soc. Trans. 36, 976-980
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 976-980
    • Hirst, J.1    King, M.S.2    Pryde, K.R.3
  • 34
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH: Ubiquinone oxidoreductase (complex I)
    • Lambert, A.J. and Brand, M.D. (2004) Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH: ubiquinone oxidoreductase (complex I). J. Biol. Chem. 279, 39414-39420
    • (2004) J. Biol. Chem , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 35
    • 4043090717 scopus 로고    scopus 로고
    • Superoxide production by NADH: Ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
    • Lambert, A.J. and Brand, M.D. (2004) Superoxide production by NADH: ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem. J. 382, 511-517
    • (2004) Biochem. J. , vol.382 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2
  • 36
    • 1942447877 scopus 로고    scopus 로고
    • The cytochrome bc1 complex: Function in the context of structure
    • Crofts, A.R. (2004) The cytochrome bc1 complex: function in the context of structure. Ann. Rev. Physiol. 66, 689-733
    • (2004) Ann. Rev. Physiol , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 37
    • 0038348619 scopus 로고    scopus 로고
    • Architecture of the Qo site of the cytochrome bc1 complex probed by superoxide production
    • Muller, F.L., Roberts, A.G., Bowman, M.K. and Kramer, D.M. (2003) Architecture of the Qo site of the cytochrome bc1 complex probed by superoxide production. Biochemistry 42, 6493-6499
    • (2003) Biochemistry , vol.42 , pp. 6493-6499
    • Muller, F.L.1    Roberts, A.G.2    Bowman, M.K.3    Kramer, D.M.4
  • 38
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller, F.L., Liu, Y. and Van Remmen, H. (2004) Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 279, 49064-49073
    • (2004) J. Biol. Chem , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 40
    • 24344508510 scopus 로고    scopus 로고
    • The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria
    • Miwa, S. and Brand, M.D. (2005) The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria. Biochim. Biophys. Acta 1709, 214-219
    • (2005) Biochim. Biophys. Acta , vol.1709 , pp. 214-219
    • Miwa, S.1    Brand, M.D.2
  • 42
    • 44949142269 scopus 로고    scopus 로고
    • The selective detection of mitochondrial superoxide by live cell imaging
    • Robinson, K.M., Janes, M.S. and Beckman, J.S. (2008) The selective detection of mitochondrial superoxide by live cell imaging. Nat. Protocols 3, 941-947
    • (2008) Nat. Protocols , vol.3 , pp. 941-947
    • Robinson, K.M.1    Janes, M.S.2    Beckman, J.S.3
  • 43
    • 0035502402 scopus 로고    scopus 로고
    • Mitochondrial uncoupling as a target for drug development for the treatment of obesity
    • Harper, J.A., Dickinson, K. and Brand, M.D. (2001) Mitochondrial uncoupling as a target for drug development for the treatment of obesity. Obes. Rev. 2, 255-265
    • (2001) Obes. Rev , vol.2 , pp. 255-265
    • Harper, J.A.1    Dickinson, K.2    Brand, M.D.3
  • 44
    • 0033787068 scopus 로고    scopus 로고
    • Skeletal muscle respiratory uncoupling prevents diet-induced obesity and insulin resistance in mice
    • Li, B., Nolte, L.A., Ju, J.S., Han, D.H., Coleman, T., Holloszy, J.O. and Semenkovich, C.F. (2000) Skeletal muscle respiratory uncoupling prevents diet-induced obesity and insulin resistance in mice. Nat. Med. 6, 1115-1120
    • (2000) Nat. Med , vol.6 , pp. 1115-1120
    • Li, B.1    Nolte, L.A.2    Ju, J.S.3    Han, D.H.4    Coleman, T.5    Holloszy, J.O.6    Semenkovich, C.F.7
  • 46
    • 58749091645 scopus 로고    scopus 로고
    • UCP1 ablation induces and abolishes diet-induced thermogenesis in mice exempt from thermal stress by living at thermoneutrality
    • Feldmann, H.M., Golozoubova, V., Cannon, B. and Nedergaard, J. (2008) UCP1 ablation induces and abolishes diet-induced thermogenesis in mice exempt from thermal stress by living at thermoneutrality. Cell. Metab. 9, 203-209
    • (2008) Cell. Metab , vol.9 , pp. 203-209
    • Feldmann, H.M.1    Golozoubova, V.2    Cannon, B.3    Nedergaard, J.4
  • 50
    • 0035875087 scopus 로고    scopus 로고
    • Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, β-cell dysfunction, and type 2 diabetes
    • Zhang, C.Y., Baffy, G., Perret, P., Krauss, S., Peroni, O., Grujic, D., Hagen, T., Vidal-Puig, A.J., Boss, O., Kim, Y.B. et al. (2001) Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, β-cell dysfunction, and type 2 diabetes. Cell 105, 745-755
    • (2001) Cell , vol.105 , pp. 745-755
    • Zhang, C.Y.1    Baffy, G.2    Perret, P.3    Krauss, S.4    Peroni, O.5    Grujic, D.6    Hagen, T.7    Vidal-Puig, A.J.8    Boss, O.9    Kim, Y.B.10
  • 51
    • 67649641804 scopus 로고    scopus 로고
    • Persistent oxidative stress due to absence of uncoupling protein 2 associated with impaired pancreatic β-cell function
    • Pi, J., Bai Y., Daniel, K.W., Liu, D., Lyght, O., Edelstein, D., Brownlee, M., Corkey, B.E. and Collins, S. (2009) Persistent oxidative stress due to absence of uncoupling protein 2 associated with impaired pancreatic β-cell function. Endocrinology 150, 3040-3048
    • (2009) Endocrinology , vol.150 , pp. 3040-3048
    • Pi, J.1    Bai, Y.2    Daniel, K.W.3    Liu, D.4    Lyght, O.5    Edelstein, D.6    Brownlee, M.7    Corkey, B.E.8    Collins, S.9


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