메뉴 건너뛰기




Volumn 526, Issue , 2013, Pages 189-217

The determination and analysis of site-specific rates of mitochondrial reactive oxygen species production

Author keywords

Complex; Electron transferring flavoprotein; Glycerol 3 phosphate dehydrogenase; Hydrogen peroxide; I; II; III; NADH; Superoxide; Ubiquinone

Indexed keywords

ANTIOXIDANT; CATALASE; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; HYDROGEN PEROXIDE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RESORUFIN; SUCCINATE DEHYDROGENASE (UBIQUINONE); SUPEROXIDE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 84879774696     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-405883-5.00012-0     Document Type: Chapter
Times cited : (76)

References (86)
  • 1
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • V. Adam-Vizi, and C. Chinopoulos Bioenergetics and the formation of mitochondrial reactive oxygen species Trends in Pharmacological Sciences 27 2006 639 645
    • (2006) Trends in Pharmacological Sciences , vol.27 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 2
    • 82355183887 scopus 로고    scopus 로고
    • Measurement of proton leak and electron leak in isolated mitochondria
    • C.L. Affourtit, C.L. Quinlan, and M.D. Brand Measurement of proton leak and electron leak in isolated mitochondria Methods in Molecular Biology 810 2012 165 182
    • (2012) Methods in Molecular Biology , vol.810 , pp. 165-182
    • Affourtit, C.L.1    Quinlan, C.L.2    Brand, M.D.3
  • 5
    • 0016681098 scopus 로고
    • Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration
    • A. Boveris, and E. Cadenas Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration FEBS Letters 54 1975 311 314
    • (1975) FEBS Letters , vol.54 , pp. 311-314
    • Boveris, A.1    Cadenas, E.2
  • 6
    • 0017407172 scopus 로고
    • Evaluation of the horseradish peroxidase-scopoletin method for the measurement of hydrogen peroxide formation in biological systems
    • A. Boveris, E. Martino, and A.O.M. Stoppani Evaluation of the horseradish peroxidase-scopoletin method for the measurement of hydrogen peroxide formation in biological systems Analytical Biochemistry 80 1977 145 158
    • (1977) Analytical Biochemistry , vol.80 , pp. 145-158
    • Boveris, A.1    Martino, E.2    Stoppani, A.O.M.3
  • 8
    • 77952541558 scopus 로고    scopus 로고
    • The sites and topology of mitochondrial superoxide production
    • M.D. Brand The sites and topology of mitochondrial superoxide production Experimental Gerontology 45 2010 466 472
    • (2010) Experimental Gerontology , vol.45 , pp. 466-472
    • Brand, M.D.1
  • 9
    • 0001231851 scopus 로고
    • Fluorometric determination of hydrogen peroxide using resorufin and peroxidase
    • G.P. Brotea, and R.J. Thibert Fluorometric determination of hydrogen peroxide using resorufin and peroxidase Microchemical Journal 37 1988 368 376
    • (1988) Microchemical Journal , vol.37 , pp. 368-376
    • Brotea, G.P.1    Thibert, R.J.2
  • 10
    • 0024023239 scopus 로고
    • Proton/electron stoichiometry of mitochondrial complex i estimated from the equilibrium thermodynamic force ratio
    • G.C. Brown, and M.D. Brand Proton/electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratio The Biochemical Journal 252 1988 473 479
    • (1988) The Biochemical Journal , vol.252 , pp. 473-479
    • Brown, G.C.1    Brand, M.D.2
  • 11
    • 0037352050 scopus 로고    scopus 로고
    • 2-Oxo acid dehydrogenase complexes in redox regulation
    • V.I. Bunik 2-Oxo acid dehydrogenase complexes in redox regulation European Journal of Biochemistry 270 2003 1036 1042
    • (2003) European Journal of Biochemistry , vol.270 , pp. 1036-1042
    • Bunik, V.I.1
  • 12
    • 0036408866 scopus 로고    scopus 로고
    • Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species
    • V.I. Bunik, and C. Sievers Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species European Journal of Biochemistry 269 2002 5004 5015
    • (2002) European Journal of Biochemistry , vol.269 , pp. 5004-5015
    • Bunik, V.I.1    Sievers, C.2
  • 13
    • 1942447877 scopus 로고    scopus 로고
    • The cytochrome bc1 complex: Function in the context of structure
    • A.R. Crofts The cytochrome bc1 complex: Function in the context of structure Annual Reviews of Physiology 66 2004 689 733
    • (2004) Annual Reviews of Physiology , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 14
  • 16
    • 0036154857 scopus 로고    scopus 로고
    • Control of mitochondrial beta-oxidation flux
    • S. Eaton Control of mitochondrial beta-oxidation flux Progress in Lipid Research 41 2002 197 239
    • (2002) Progress in Lipid Research , vol.41 , pp. 197-239
    • Eaton, S.1
  • 17
    • 0017193363 scopus 로고
    • Mitochondrial cytochrome b-c complex: Its oxidation-reduction components and their stoichiometry
    • M. Erecinska, D.F. Wilson, and Y. Miyata Mitochondrial cytochrome b-c complex: Its oxidation-reduction components and their stoichiometry Archives of Biochemistry and Biophysics 177 1976 133 143
    • (1976) Archives of Biochemistry and Biophysics , vol.177 , pp. 133-143
    • Erecinska, M.1    Wilson, D.F.2    Miyata, Y.3
  • 18
    • 0005418447 scopus 로고
    • Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase
    • W.R. Frisell, and C.G. Mackenzie Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase The Journal of Biological Chemistry 237 1962 94 98
    • (1962) The Journal of Biological Chemistry , vol.237 , pp. 94-98
    • Frisell, W.R.1    MacKenzie, C.G.2
  • 19
    • 0035975713 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations, oxidative stress, and aging
    • T. Golden, and S. Melov Mitochondrial DNA mutations, oxidative stress, and aging Mechanisms of Ageing and Development 122 2001 1577 1589
    • (2001) Mechanisms of Ageing and Development , vol.122 , pp. 1577-1589
    • Golden, T.1    Melov, S.2
  • 20
    • 0019332510 scopus 로고
    • Studies on electron transfer from general acyl-CoA dehydrogenase to electron transfer flavoprotein
    • C.L. Hall, and J.D. Lambeth Studies on electron transfer from general acyl-CoA dehydrogenase to electron transfer flavoprotein The Journal of Biological Chemistry 255 1980 3591 3595
    • (1980) The Journal of Biological Chemistry , vol.255 , pp. 3591-3595
    • Hall, C.L.1    Lambeth, J.D.2
  • 21
    • 0142210179 scopus 로고    scopus 로고
    • Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria
    • D. Han, R. Canali, D. Rettori, and N. Kaplowitz Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria Molecular Pharmacology 64 2003 1136 1144
    • (2003) Molecular Pharmacology , vol.64 , pp. 1136-1144
    • Han, D.1    Canali, R.2    Rettori, D.3    Kaplowitz, N.4
  • 23
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • D. Harman Aging: A theory based on free radical and radiation chemistry Journal of Gerontology 11 1956 298 300
    • (1956) Journal of Gerontology , vol.11 , pp. 298-300
    • Harman, D.1
  • 24
    • 0021160336 scopus 로고
    • A quantitative fluorimetric assay for the determination of oxidant production by polymorphonuclear leukocytes: Its use in the simultaneous fluorimetric assay of cellular activation processes
    • P.A. Hyslop, and L.A. Sklar A quantitative fluorimetric assay for the determination of oxidant production by polymorphonuclear leukocytes: Its use in the simultaneous fluorimetric assay of cellular activation processes Analytical Biochemistry 141 1984 280 286
    • (1984) Analytical Biochemistry , vol.141 , pp. 280-286
    • Hyslop, P.A.1    Sklar, L.A.2
  • 25
    • 0021099782 scopus 로고
    • Purification and characterization of 2-methyl-branched chain acyl coenzyme A dehydrogenase, an enzyme involved in the isoleucine and valine metabolism, from rat liver mitochondria
    • Y. Ikeda, and K. Tanaka Purification and characterization of 2-methyl-branched chain acyl coenzyme A dehydrogenase, an enzyme involved in the isoleucine and valine metabolism, from rat liver mitochondria The Journal of Biological Chemistry 258 1983 9477 9487
    • (1983) The Journal of Biological Chemistry , vol.258 , pp. 9477-9487
    • Ikeda, Y.1    Tanaka, K.2
  • 26
    • 0021111508 scopus 로고
    • Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria
    • Y. Ikeda, and K. Tanaka Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria The Journal of Biological Chemistry 258 1983 1077 1085
    • (1983) The Journal of Biological Chemistry , vol.258 , pp. 1077-1085
    • Ikeda, Y.1    Tanaka, K.2
  • 27
    • 40949126440 scopus 로고    scopus 로고
    • Mitochondrial complex III regulates hypoxic activation of HIF
    • T. Klimova, and N.S. Chandel Mitochondrial complex III regulates hypoxic activation of HIF Cell Death and Differentiation 15 2008 660 666
    • (2008) Cell Death and Differentiation , vol.15 , pp. 660-666
    • Klimova, T.1    Chandel, N.S.2
  • 28
    • 0014764841 scopus 로고
    • Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane
    • M. Klingenberg Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane European Journal of Biochemistry 13 1970 247 252
    • (1970) European Journal of Biochemistry , vol.13 , pp. 247-252
    • Klingenberg, M.1
  • 29
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • S.S. Korshunov, V.P. Skulachev, and A.A. Starkov High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria FEBS Letters 416 1997 15 18
    • (1997) FEBS Letters , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 30
    • 0036903625 scopus 로고    scopus 로고
    • Complex I-mediated reactive oxygen species generation: Modulation by cytochrome c and NAD(P)+ oxidation-reduction state
    • Y. Kushnareva, A.N. Murphy, and A. Andreyev Complex I-mediated reactive oxygen species generation: Modulation by cytochrome c and NAD(P)+ oxidation-reduction state The Biochemical Journal 368 2002 545 553
    • (2002) The Biochemical Journal , vol.368 , pp. 545-553
    • Kushnareva, Y.1    Murphy, A.N.2    Andreyev, A.3
  • 31
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH: Ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • L. Kussmaul, and J. Hirst The mechanism of superoxide production by NADH: Ubiquinone oxidoreductase (complex I) from bovine heart mitochondria Proceedings of the National Academy of Sciences of the United States of America 103 2006 7607 7612
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 32
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • A.J. Lambert, and M.D. Brand Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I) The Journal of Biological Chemistry 279 2004 39414 39420
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 33
    • 4043090717 scopus 로고    scopus 로고
    • Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
    • A.J. Lambert, and M.D. Brand Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane The Biochemical Journal 382 2004 511 517
    • (2004) The Biochemical Journal , vol.382 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2
  • 34
    • 0022980720 scopus 로고
    • The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver
    • A.C. Lenich, and S.I. Goodman The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver The Journal of Biological Chemistry 261 1986 4090 4096
    • (1986) The Journal of Biological Chemistry , vol.261 , pp. 4090-4096
    • Lenich, A.C.1    Goodman, S.I.2
  • 35
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Y. Liu, G. Fiskum, and D. Schubert Generation of reactive oxygen species by the mitochondrial electron transport chain Journal of Neurochemistry 80 2002 780 787
    • (2002) Journal of Neurochemistry , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 36
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • J.M. McCord, and I. Fridovich Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) The Journal of Biological Chemistry 244 1969 6049 6055
    • (1969) The Journal of Biological Chemistry , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 37
    • 25444513733 scopus 로고    scopus 로고
    • Enhanced sensitivity and precision in an enzyme-linked immunosorbent assay with fluorogenic substrates compared with commonly used chromogenic substrates
    • Y. Meng, K. High, J. Antonello, M.W. Washabaugh, and Q. Zhao Enhanced sensitivity and precision in an enzyme-linked immunosorbent assay with fluorogenic substrates compared with commonly used chromogenic substrates Analytical Biochemistry 345 2005 227 236
    • (2005) Analytical Biochemistry , vol.345 , pp. 227-236
    • Meng, Y.1    High, K.2    Antonello, J.3    Washabaugh, M.W.4    Zhao, Q.5
  • 38
    • 0037044847 scopus 로고    scopus 로고
    • Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
    • K.R. Messner, and J.A. Imlay Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase The Journal of Biological Chemistry 277 2002 42563 42571
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 42563-42571
    • Messner, K.R.1    Imlay, J.A.2
  • 39
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • P. Mitchell The protonmotive Q cycle: A general formulation FEBS Letters 59 1975 137 139
    • (1975) FEBS Letters , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 43
    • 38749087624 scopus 로고    scopus 로고
    • High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates
    • F.L. Muller, Y. Liu, M.A. Abdul-Ghani, M.S. Lustgarten, A. Bhattacharya, and Y.C. Jang High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates The Biochemical Journal 409 2008 491 499
    • (2008) The Biochemical Journal , vol.409 , pp. 491-499
    • Muller, F.L.1    Liu, Y.2    Abdul-Ghani, M.A.3    Lustgarten, M.S.4    Bhattacharya, A.5    Jang, Y.C.6
  • 45
    • 0019073929 scopus 로고
    • The metabolic fate of mitochondrial hydrogen peroxide
    • H. Nohl, and W. Jordan The metabolic fate of mitochondrial hydrogen peroxide European Journal of Biochemistry 111 1980 203 210
    • (1980) European Journal of Biochemistry , vol.111 , pp. 203-210
    • Nohl, H.1    Jordan, W.2
  • 46
    • 78149469831 scopus 로고    scopus 로고
    • New insights into the superoxide generation sites in bovine heart NADH-ubiquinone oxidoreductase (Complex I): The significance of protein-associated ubiquinone and the dynamic shifting of generation sites between semiflavin and semiquinone radicals
    • S.T. Ohnishi, K. Shinzawa-Itoh, K. Ohta, S. Yoshikawa, and T. Ohnishi New insights into the superoxide generation sites in bovine heart NADH-ubiquinone oxidoreductase (Complex I): The significance of protein-associated ubiquinone and the dynamic shifting of generation sites between semiflavin and semiquinone radicals Biochimica et Biophysica Acta 1797 2010 1901 1909
    • (2010) Biochimica et Biophysica Acta , vol.1797 , pp. 1901-1909
    • Ohnishi, S.T.1    Shinzawa-Itoh, K.2    Ohta, K.3    Yoshikawa, S.4    Ohnishi, T.5
  • 47
    • 84871139444 scopus 로고    scopus 로고
    • A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase
    • A.L. Orr, C.L. Quinlan, I.V. Perevoshchikova, and M.D. Brand A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase The Journal of Biological Chemistry 287 2012 42921 42935
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 42921-42935
    • Orr, A.L.1    Quinlan, C.L.2    Perevoshchikova, I.V.3    Brand, M.D.4
  • 48
    • 76049086567 scopus 로고    scopus 로고
    • Contribution of the FAD and quinone binding sites to the production of reactive oxygen species from Ascaris suum mitochondrial complex II
    • M.P. Paranagama, K. Sakamoto, H. Amino, M. Awano, H. Miyoshi, and K. Kita Contribution of the FAD and quinone binding sites to the production of reactive oxygen species from Ascaris suum mitochondrial complex II Mitochondrion 10 2010 158 165
    • (2010) Mitochondrion , vol.10 , pp. 158-165
    • Paranagama, M.P.1    Sakamoto, K.2    Amino, H.3    Awano, M.4    Miyoshi, H.5    Kita, K.6
  • 49
    • 84878009179 scopus 로고    scopus 로고
    • Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle
    • 10.1016/j.freeradbiomed.2013.04.006 In press
    • I.V. Perevoshchikova, C.L. Quinlan, A.L. Orr, and M.D. Brand Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle Free Radical Biology & Medicine 2013 10.1016/j. freeradbiomed.2013.04.006 In press.
    • (2013) Free Radical Biology & Medicine
    • Perevoshchikova, I.V.1    Quinlan, C.L.2    Orr, A.L.3    Brand, M.D.4
  • 50
    • 79955977892 scopus 로고    scopus 로고
    • Superoxide is produced by the reduced flavin in mitochondrial complex I: A single, unified mechanism that applies during both forward and reverse electron transfer
    • K.R. Pryde, and J. Hirst Superoxide is produced by the reduced flavin in mitochondrial complex I: A single, unified mechanism that applies during both forward and reverse electron transfer The Journal of Biological Chemistry 286 2011 18056 18065
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 18056-18065
    • Pryde, K.R.1    Hirst, J.2
  • 53
    • 84867401800 scopus 로고    scopus 로고
    • Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reporters
    • C.L. Quinlan, J.R. Treberg, I.V. Perevoshchikova, A.L. Orr, and M.D. Brand Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reporters Free Radical Biology & Medicine 53 2012 1807 1817
    • (2012) Free Radical Biology & Medicine , vol.53 , pp. 1807-1817
    • Quinlan, C.L.1    Treberg, J.R.2    Perevoshchikova, I.V.3    Orr, A.L.4    Brand, M.D.5
  • 55
    • 0023283867 scopus 로고
    • Reactions of electron-transfer flavoprotein and electron-transfer flavoprotein: Ubiquinone oxidoreductase
    • R.R. Ramsay, D.J. Steenkamp, and M. Husain Reactions of electron-transfer flavoprotein and electron-transfer flavoprotein: Ubiquinone oxidoreductase The Biochemical Journal 241 1987 883 892
    • (1987) The Biochemical Journal , vol.241 , pp. 883-892
    • Ramsay, R.R.1    Steenkamp, D.J.2    Husain, M.3
  • 56
  • 57
    • 84861542507 scopus 로고    scopus 로고
    • Mechanism of superoxide and hydrogen peroxide generation by human electron-transfer flavoprotein and pathological variants
    • J.V. Rodrigues, and C.M. Gomes Mechanism of superoxide and hydrogen peroxide generation by human electron-transfer flavoprotein and pathological variants Free Radical Biology & Medicine 53 2012 12 19
    • (2012) Free Radical Biology & Medicine , vol.53 , pp. 12-19
    • Rodrigues, J.V.1    Gomes, C.M.2
  • 58
    • 67749111889 scopus 로고    scopus 로고
    • Membrane potential greatly enhances superoxide generation by the cytochrome bc1 complex reconstituted into phospholipid vesicles
    • H. Rottenberg, R. Covian, and B.L. Trumpower Membrane potential greatly enhances superoxide generation by the cytochrome bc1 complex reconstituted into phospholipid vesicles The Journal of Biological Chemistry 284 2009 19203 19210
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 19203-19210
    • Rottenberg, H.1    Covian, R.2    Trumpower, B.L.3
  • 59
    • 0020642791 scopus 로고
    • 2 production by macrophages and neutrophils with homovanillic acid and horse-radish peroxidase
    • 2 production by macrophages and neutrophils with homovanillic acid and horse-radish peroxidase Journal of Immunological Methods 63 1983 347 357
    • (1983) Journal of Immunological Methods , vol.63 , pp. 347-357
    • Ruch, W.1    Cooper, P.H.2    Baggiolini, M.3
  • 60
    • 0017691203 scopus 로고
    • A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway
    • F.J. Ruzicka, and H. Beinert A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway The Journal of Biological Chemistry 252 1977 8440 8445
    • (1977) The Journal of Biological Chemistry , vol.252 , pp. 8440-8445
    • Ruzicka, F.J.1    Beinert, H.2
  • 61
    • 33745635338 scopus 로고    scopus 로고
    • Mitochondrial NADPH, transhydrogenase and disease
    • J. Rydstrom Mitochondrial NADPH, transhydrogenase and disease Biochimica et Biophysica Acta 1757 2006 721 726
    • (2006) Biochimica et Biophysica Acta , vol.1757 , pp. 721-726
    • Rydstrom, J.1
  • 62
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • F.Q. Schafer, and G.R. Buettner Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple Free Radical Biology & Medicine 30 2001 1191 1212
    • (2001) Free Radical Biology & Medicine , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 63
    • 34748850786 scopus 로고    scopus 로고
    • Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress
    • T.J. Schulz, K. Zarse, A. Voigt, N. Urban, M. Birringer, and M. Ristow Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress Cell Metabolism 6 2007 280 293
    • (2007) Cell Metabolism , vol.6 , pp. 280-293
    • Schulz, T.J.1    Zarse, K.2    Voigt, A.3    Urban, N.4    Birringer, M.5    Ristow, M.6
  • 64
    • 0032834347 scopus 로고    scopus 로고
    • H2O2 detection from intact mitochondria as a measure for one-electron reduction of dioxygen requires a non-invasive assay system
    • K. Staniek, and H. Nohl H2O2 detection from intact mitochondria as a measure for one-electron reduction of dioxygen requires a non-invasive assay system Biochimica et Biophysica Acta: Bioenergetics 1413 1999 70 80
    • (1999) Biochimica et Biophysica Acta: Bioenergetics , vol.1413 , pp. 70-80
    • Staniek, K.1    Nohl, H.2
  • 65
    • 0042433242 scopus 로고    scopus 로고
    • 2 production by membrane potential and NAD(P)H redox state
    • 2 production by membrane potential and NAD(P)H redox state Journal of Neurochemistry 86 2003 1101 1107
    • (2003) Journal of Neurochemistry , vol.86 , pp. 1101-1107
    • Starkov, A.A.1    Fiskum, G.2
  • 67
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • J. St-Pierre, J.A. Buckingham, S.J. Roebuck, and M.D. Brand Topology of superoxide production from different sites in the mitochondrial electron transport chain The Journal of Biological Chemistry 277 2002 44784 44790
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 68
    • 21244503033 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial respiratory membrane protein complex II
    • F. Sun, X. Huo, Y. Zhai, A. Wang, J. Xu, and D. Su Crystal structure of mitochondrial respiratory membrane protein complex II Cell 121 2005 1043 1057
    • (2005) Cell , vol.121 , pp. 1043-1057
    • Sun, F.1    Huo, X.2    Zhai, Y.3    Wang, A.4    Xu, J.5    Su, D.6
  • 70
    • 79955966782 scopus 로고    scopus 로고
    • A model of the proton translocation mechanism of complex i
    • J.R. Treberg, and M.D. Brand A model of the proton translocation mechanism of complex I The Journal of Biological Chemistry 286 2011 17579 17584
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 17579-17584
    • Treberg, J.R.1    Brand, M.D.2
  • 71
    • 77953565915 scopus 로고    scopus 로고
    • Hydrogen peroxide efflux from muscle mitochondria underestimates matrix superoxide production - A correction using glutathione depletion
    • J.R. Treberg, C.L. Quinlan, and M.D. Brand Hydrogen peroxide efflux from muscle mitochondria underestimates matrix superoxide production - A correction using glutathione depletion The FEBS Journal 277 2010 2766 2778
    • (2010) The FEBS Journal , vol.277 , pp. 2766-2778
    • Treberg, J.R.1    Quinlan, C.L.2    Brand, M.D.3
  • 72
    • 79961008706 scopus 로고    scopus 로고
    • Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I)
    • J.R. Treberg, C.L. Quinlan, and M.D. Brand Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I) The Journal of Biological Chemistry 286 2011 27103 27110
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 27103-27110
    • Treberg, J.R.1    Quinlan, C.L.2    Brand, M.D.3
  • 75
    • 0018699357 scopus 로고
    • Electron and proton transport in the ubiquinone cytochrome b-c2 oxidoreductase of Rhodopseudomonas sphaeroides. Patterns of binding and inhibition by antimycin
    • W.H. Van den Berg, R.C. Prince, C.L. Bashford, K.I. Takamiya, W.D. Bonner Jr., and P.L. Dutton Electron and proton transport in the ubiquinone cytochrome b-c2 oxidoreductase of Rhodopseudomonas sphaeroides. Patterns of binding and inhibition by antimycin The Journal of Biological Chemistry 254 1979 8594 8604
    • (1979) The Journal of Biological Chemistry , vol.254 , pp. 8594-8604
    • Van Den Berg, W.H.1    Prince, R.C.2    Bashford, C.L.3    Takamiya, K.I.4    Bonner, Jr.W.D.5    Dutton, P.L.6
  • 76
    • 17144366976 scopus 로고    scopus 로고
    • Generation of superoxide-radical by the NADH:ubiquinone oxidoreductase of heart mitochondria
    • A.D. Vinogradov, and V.G. Grivennikova Generation of superoxide-radical by the NADH:ubiquinone oxidoreductase of heart mitochondria Biochemistry (Moscow) 70 2005 120 127
    • (2005) Biochemistry (Moscow) , vol.70 , pp. 120-127
    • Vinogradov, A.D.1    Grivennikova, V.G.2
  • 77
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi(m)-Dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • T.V. Votyakova, and I.J. Reynolds DeltaPsi(m)-Dependent and -independent production of reactive oxygen species by rat brain mitochondria Journal of Neurochemistry 79 2001 266 277
    • (2001) Journal of Neurochemistry , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 78
    • 78149455629 scopus 로고    scopus 로고
    • The electron transfer flavoprotein: Ubiquinone oxidoreductases
    • N.J. Watmough, and F.E. Frerman The electron transfer flavoprotein: Ubiquinone oxidoreductases Biochimica et Biophysica Acta 1797 2010 1910 1916
    • (2010) Biochimica et Biophysica Acta , vol.1797 , pp. 1910-1916
    • Watmough, N.J.1    Frerman, F.E.2
  • 80
    • 0023832894 scopus 로고
    • Electron conduction between b cytochromes of the mitochondrial respiratory chain in the presence of antimycin plus myxothiazol
    • I.C. West, P. Mitchell, and P.R. Rich Electron conduction between b cytochromes of the mitochondrial respiratory chain in the presence of antimycin plus myxothiazol Biochimica et Biophysica Acta 933 1988 35 41
    • (1988) Biochimica et Biophysica Acta , vol.933 , pp. 35-41
    • West, I.C.1    Mitchell, P.2    Rich, P.R.3
  • 81
    • 77955385260 scopus 로고    scopus 로고
    • Mitochondrial dysfunction: A potential link between neuroinflammation and neurodegeneration?
    • M.E. Witte, J.J. Geurts, H.E. de Vries, P. van der Valk, and J. van Horssen Mitochondrial dysfunction: A potential link between neuroinflammation and neurodegeneration? Mitochondrion 10 2010 411 418
    • (2010) Mitochondrion , vol.10 , pp. 411-418
    • Witte, M.E.1    Geurts, J.J.2    De Vries, H.E.3    Van Der Valk, P.4    Van Horssen, J.5
  • 83
    • 84859475161 scopus 로고    scopus 로고
    • Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolism to induce a transient ROS signal
    • K. Zarse, S. Schmeisser, M. Groth, S. Priebe, G. Beuster, and D. Kuhlow Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolism to induce a transient ROS signal Cell Metabolism 15 2012 451 465
    • (2012) Cell Metabolism , vol.15 , pp. 451-465
    • Zarse, K.1    Schmeisser, S.2    Groth, M.3    Priebe, S.4    Beuster, G.5    Kuhlow, D.6
  • 84
    • 33750814320 scopus 로고    scopus 로고
    • Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool
    • J. Zhang, F.E. Frerman, and J.J. Kim Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool Proceedings of the National Academy of Sciences of the United States America 103 2006 16212 16217
    • (2006) Proceedings of the National Academy of Sciences of the United States America , vol.103 , pp. 16212-16217
    • Zhang, J.1    Frerman, F.E.2    Kim, J.J.3
  • 85
    • 0032545269 scopus 로고    scopus 로고
    • Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria
    • L. Zhang, L. Yu, and C.A. Yu Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria The Journal of Biological Chemistry 273 1998 33972 33976
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 33972-33976
    • Zhang, L.1    Yu, L.2    Yu, C.A.3
  • 86
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • M. Zhou, Z. Diwu, N. Panchuk-Voloshina, and R.P. Haugland A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases Analytical Biochemistry 253 1997 162 168
    • (1997) Analytical Biochemistry , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.