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Volumn 45, Issue 7-8, 2010, Pages 466-472

The sites and topology of mitochondrial superoxide production

Author keywords

Complex I; Complex III; Electron transport; ETFQOR; Glycerol phosphate dehydrogenase; Reactive oxygen species; ROS; Semiquinone

Indexed keywords

ADENOSINE TRIPHOSPHATE; CITRININ; ELECTRON TRANSFERRING FLAVOPROTEIN; ELECTRON TRANSFERRING FLAVOPROTEIN:Q OXIDOREDUCTASE; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; MITOCHONDRIAL ENZYME; MITOCHONDRIAL SUPEROXIDE; OXIDOREDUCTASE; OXOGLUTARATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE; PYRUVIC ACID; QUERCETIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUPEROXIDE; SUPEROXIDE DISMUTASE; UBIQUINOL CYTOCHROME C REDUCTASE; UBIQUINONE; UNCLASSIFIED DRUG;

EID: 77952541558     PISSN: 05315565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exger.2010.01.003     Document Type: Article
Times cited : (914)

References (113)
  • 1
    • 17144422877 scopus 로고    scopus 로고
    • Mitochondrial metabolism of reactive oxygen species
    • Andreyev A.Y., Kushnareva Y.E., Starkov A.A. Mitochondrial metabolism of reactive oxygen species. Biochemistry 2005, 70:200-214.
    • (2005) Biochemistry , vol.70 , pp. 200-214
    • Andreyev, A.Y.1    Kushnareva, Y.E.2    Starkov, A.A.3
  • 2
    • 0242582202 scopus 로고    scopus 로고
    • Synchronized whole cell oscillations in mitochondrial metabolism triggered by a local release of reactive oxygen species in cardiac myocytes
    • Aon M.A., Cortassa S., Marban E., O'Rourke B. Synchronized whole cell oscillations in mitochondrial metabolism triggered by a local release of reactive oxygen species in cardiac myocytes. J. Biol. Chem. 2003, 278:44735-44744.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44735-44744
    • Aon, M.A.1    Cortassa, S.2    Marban, E.3    O'Rourke, B.4
  • 4
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja G. Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J. Bioenerg. Biomembr. 1999, 31:347-366.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 347-366
    • Barja, G.1
  • 5
    • 0036328867 scopus 로고    scopus 로고
    • 2 generation in isolated mitochondria
    • 2 generation in isolated mitochondria. J. Bioenerg. Biomembr. 2002, 34:227-233.
    • (2002) J. Bioenerg. Biomembr. , vol.34 , pp. 227-233
    • Barja, G.1
  • 7
    • 0033522924 scopus 로고    scopus 로고
    • Titrating the effects of mitochondrial complex I impairment in the cell physiology
    • Barrientos A., Moraes C.T. Titrating the effects of mitochondrial complex I impairment in the cell physiology. J. Biol. Chem. 1999, 274:16188-16197.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16188-16197
    • Barrientos, A.1    Moraes, C.T.2
  • 8
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman K.B., Ames B.N. The free radical theory of aging matures. Physiol. Rev. 1998, 78:547-581.
    • (1998) Physiol. Rev. , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 9
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris A., Chance B. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem. J. 1973, 134:707-716.
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 10
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A., Oshino N., Chance B. The cellular production of hydrogen peroxide. Biochem. J. 1972, 128:617-630.
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 11
    • 0033785071 scopus 로고    scopus 로고
    • Uncoupling to survive? The role of mitochondrial inefficiency in ageing
    • Brand M.D. Uncoupling to survive? The role of mitochondrial inefficiency in ageing. Exp. Gerontol. 2000, 35:811-820.
    • (2000) Exp. Gerontol. , vol.35 , pp. 811-820
    • Brand, M.D.1
  • 13
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas E., Davies K.J. Mitochondrial free radical generation, oxidative stress, and aging. Free Radical Biol. Med. 2000, 29:222-230.
    • (2000) Free Radical Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 14
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • Cadenas E., Boveris A., Ragan C.I., Stoppani A.O. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch. Biochem. Biophys. 1977, 180:248-257.
    • (1977) Arch. Biochem. Biophys. , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 16
    • 1342323673 scopus 로고    scopus 로고
    • Oxidative stress, toxicology, and pharmacology of CYP2E1
    • Caro A.A., Cederbaum A.I. Oxidative stress, toxicology, and pharmacology of CYP2E1. Annu. Rev. Pharmacol. Toxicol. 2004, 44:27-42.
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 27-42
    • Caro, A.A.1    Cederbaum, A.I.2
  • 17
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 1979, 59:527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 19
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: central role of complex III
    • Chen Q., Vazquez E.J., Moghaddas S., Hoppel C.L., Lesnefsky E.J. Production of reactive oxygen species by mitochondria: central role of complex III. J. Biol. Chem. 2003, 278:36027-36031.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 21
    • 0032490114 scopus 로고    scopus 로고
    • Inhibitors of NADH-ubiquinone reductase: an overview
    • Degli Esposti M. Inhibitors of NADH-ubiquinone reductase: an overview. Biochim. Biophys. Acta 1998, 1364:222-235.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 222-235
    • Degli Esposti, M.1
  • 23
    • 0036244950 scopus 로고    scopus 로고
    • Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide
    • Drahota Z., Chowdhury S.K., Floryk D., Mracek T., Wilhelm J., Rauchova H., Lenaz G., Houstek J. Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide. J. Bioenerg. Biomembr. 2002, 34:105-113.
    • (2002) J. Bioenerg. Biomembr. , vol.34 , pp. 105-113
    • Drahota, Z.1    Chowdhury, S.K.2    Floryk, D.3    Mracek, T.4    Wilhelm, J.5    Rauchova, H.6    Lenaz, G.7    Houstek, J.8
  • 25
    • 0017074295 scopus 로고
    • 566, and their relationship to ubiquinone and the iron-sulfur centers S-1 (+N-2) and S-3
    • 566, and their relationship to ubiquinone and the iron-sulfur centers S-1 (+N-2) and S-3. Arch. Biochem. Biophys. 1976, 174:143-157.
    • (1976) Arch. Biochem. Biophys. , vol.174 , pp. 143-157
    • Erecinska, M.1    Wilson, D.F.2
  • 26
    • 0037441390 scopus 로고    scopus 로고
    • External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide
    • Fang J., Beattie D.S. External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide. Free Radical Biol. Med. 2003, 34:478-488.
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 478-488
    • Fang, J.1    Beattie, D.S.2
  • 27
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T., Holbrook N.J. Oxidants, oxidative stress and the biology of ageing. Nature 2000, 408:239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 28
    • 0037155880 scopus 로고    scopus 로고
    • Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase
    • Gazaryan I.G., Krasnikov B.F., Ashby G.A., Thorneley R.N., Kristal B.S., Brown A.M. Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase. J. Biol. Chem. 2002, 277:10064-10072.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10064-10072
    • Gazaryan, I.G.1    Krasnikov, B.F.2    Ashby, G.A.3    Thorneley, R.N.4    Kristal, B.S.5    Brown, A.M.6
  • 29
    • 0035929367 scopus 로고    scopus 로고
    • The site of production of superoxide radical in mitochondrial complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2
    • Genova M.L., Ventura B., Giuliano G., Bovina C., Formiggini G., Parenti Castelli G., Lenaz G. The site of production of superoxide radical in mitochondrial complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2. FEBS Lett. 2001, 505:364-368.
    • (2001) FEBS Lett. , vol.505 , pp. 364-368
    • Genova, M.L.1    Ventura, B.2    Giuliano, G.3    Bovina, C.4    Formiggini, G.5    Parenti Castelli, G.6    Lenaz, G.7
  • 30
    • 0042734428 scopus 로고    scopus 로고
    • Oxidative stress and aging: beyond correlation
    • Golden T.R., Hinerfeld D.A., Melov S. Oxidative stress and aging: beyond correlation. Aging Cell 2002, 1:117-123.
    • (2002) Aging Cell , vol.1 , pp. 117-123
    • Golden, T.R.1    Hinerfeld, D.A.2    Melov, S.3
  • 31
    • 3142777700 scopus 로고    scopus 로고
    • Shift in the localization of sites of hydrogen peroxide production in brain mitochondria by mitochondrial stress
    • Gyulkhandanyan A.V., Pennefather P.S. Shift in the localization of sites of hydrogen peroxide production in brain mitochondria by mitochondrial stress. J. Neurochem. 2004, 90:405-421.
    • (2004) J. Neurochem. , vol.90 , pp. 405-421
    • Gyulkhandanyan, A.V.1    Pennefather, P.S.2
  • 33
    • 0035863011 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
    • Han D., Williams E., Cadenas E. Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space. Biochem. J. 2001, 353:411-416.
    • (2001) Biochem. J. , vol.353 , pp. 411-416
    • Han, D.1    Williams, E.2    Cadenas, E.3
  • 34
    • 0142210179 scopus 로고    scopus 로고
    • Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria
    • Han D., Canali R., Rettori D., Kaplowitz N. Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria. Mol. Pharmacol. 2003, 64:1136-1144.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1136-1144
    • Han, D.1    Canali, R.2    Rettori, D.3    Kaplowitz, N.4
  • 36
    • 0015319592 scopus 로고
    • The biologic clock: the mitochondria?
    • Harman D. The biologic clock: the mitochondria?. J. Am. Geriat. Soc. 1972, 20:145-147.
    • (1972) J. Am. Geriat. Soc. , vol.20 , pp. 145-147
    • Harman, D.1
  • 37
    • 0030793931 scopus 로고    scopus 로고
    • Sites and mechanisms responsible for the low rate of free radical production of heart mitochondria in the long-lived pigeon
    • Herrero A., Barja G. Sites and mechanisms responsible for the low rate of free radical production of heart mitochondria in the long-lived pigeon. Mech. Ageing Dev. 1997, 98:95-111.
    • (1997) Mech. Ageing Dev. , vol.98 , pp. 95-111
    • Herrero, A.1    Barja, G.2
  • 38
    • 0034467677 scopus 로고    scopus 로고
    • Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria
    • Herrero A., Barja G. Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria. J. Bioenerg. Biomembr. 2000, 32:609-615.
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 609-615
    • Herrero, A.1    Barja, G.2
  • 39
    • 0014217470 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome b region of the respiratory chain of beef heart submitochondrial particles
    • Hinkle P.C., Butow R.A., Racker E., Chance B. Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome b region of the respiratory chain of beef heart submitochondrial particles. J. Biol. Chem. 1967, 242:5169-5173.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5169-5173
    • Hinkle, P.C.1    Butow, R.A.2    Racker, E.3    Chance, B.4
  • 40
    • 53849099653 scopus 로고    scopus 로고
    • The production of reactive oxygen species by complex I
    • Hirst J., King M.S., Pryde K.R. The production of reactive oxygen species by complex I. Biochem. Soc. Trans. 2008, 36:976-980.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 976-980
    • Hirst, J.1    King, M.S.2    Pryde, K.R.3
  • 41
    • 0032571387 scopus 로고    scopus 로고
    • Reduced fertility in female mice lacking copper-zinc superoxide dismutase
    • Ho Y.S., Gargano M., Cao J., Bronson R.T., Heimler I., Hutz R.J. Reduced fertility in female mice lacking copper-zinc superoxide dismutase. J. Biol. Chem. 1998, 273:7765-7769.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7765-7769
    • Ho, Y.S.1    Gargano, M.2    Cao, J.3    Bronson, R.T.4    Heimler, I.5    Hutz, R.J.6
  • 42
    • 67650248980 scopus 로고    scopus 로고
    • Oxygen sensitivity of mitochondrial reactive oxygen species generation depends on metabolic conditions
    • Hoffman D.L., Brookes P.S. Oxygen sensitivity of mitochondrial reactive oxygen species generation depends on metabolic conditions. J. Biol. Chem. 2009, 284:16236-16245.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16236-16245
    • Hoffman, D.L.1    Brookes, P.S.2
  • 44
    • 33747149006 scopus 로고    scopus 로고
    • Bioenergetic analysis of cerebellar granule neurons undergoing apoptosis by potassium/serum deprivation
    • Jekabsons M.B., Nicholls D.G. Bioenergetic analysis of cerebellar granule neurons undergoing apoptosis by potassium/serum deprivation. Cell Death Differ. 2006, 13:1595-1610.
    • (2006) Cell Death Differ. , vol.13 , pp. 1595-1610
    • Jekabsons, M.B.1    Nicholls, D.G.2
  • 45
    • 0014010888 scopus 로고
    • Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation
    • Jensen P.K. Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation. Biochim. Biophys. Acta 1966, 122:157-166.
    • (1966) Biochim. Biophys. Acta , vol.122 , pp. 157-166
    • Jensen, P.K.1
  • 46
    • 25844520458 scopus 로고    scopus 로고
    • Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism
    • Jezek P., Hlavata L. Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism. Int. J. Biochem. Cell Biol. 2005, 37:2478-2503.
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 2478-2503
    • Jezek, P.1    Hlavata, L.2
  • 47
    • 0141684565 scopus 로고    scopus 로고
    • NADH-ubiquinone oxidoreductase: substrate-dependent oxygen turnover to superoxide anion as a function of flavin mononucleotide
    • Johnson J.E., Choksi K., Widger W.R. NADH-ubiquinone oxidoreductase: substrate-dependent oxygen turnover to superoxide anion as a function of flavin mononucleotide. Mitochondrion 2003, 3:97-110.
    • (2003) Mitochondrion , vol.3 , pp. 97-110
    • Johnson, J.E.1    Choksi, K.2    Widger, W.R.3
  • 48
    • 34249781383 scopus 로고    scopus 로고
    • 'Mild uncoupling' does not decrease mitochondrial superoxide levels in cultured cerebellar granule neurons but decreases spare respiratory capacity and increases toxicity to glutamate and oxidative stress
    • Johnson-Cadwell L.I., Jekabsons M.B., Wang A., Polster B.M., Nicholls D.G. 'Mild uncoupling' does not decrease mitochondrial superoxide levels in cultured cerebellar granule neurons but decreases spare respiratory capacity and increases toxicity to glutamate and oxidative stress. J. Neurochem. 2007, 101:1619-1631.
    • (2007) J. Neurochem. , vol.101 , pp. 1619-1631
    • Johnson-Cadwell, L.I.1    Jekabsons, M.B.2    Wang, A.3    Polster, B.M.4    Nicholls, D.G.5
  • 49
    • 0037438948 scopus 로고    scopus 로고
    • No increase in lifespan in Caenorhabditis elegans upon treatment with the superoxide dismutase mimetic EUK-8
    • Keaney M., Gems D. No increase in lifespan in Caenorhabditis elegans upon treatment with the superoxide dismutase mimetic EUK-8. Free Radical Biol. Med. 2003, 34:277-282.
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 277-282
    • Keaney, M.1    Gems, D.2
  • 50
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov S.S., Skulachev V.P., Starkov A.A. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 1997, 416:15-18.
    • (1997) FEBS Lett. , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 52
    • 0027365312 scopus 로고
    • Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species
    • Ku H.H., Brunk U.T., Sohal R.S. Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species. Free Radical Biol. Med. 1993, 15:621-627.
    • (1993) Free Radical Biol. Med. , vol.15 , pp. 621-627
    • Ku, H.H.1    Brunk, U.T.2    Sohal, R.S.3
  • 53
  • 55
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • Kussmaul L., Hirst J. The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc. Natl. Acad. Sci. USA 2006, 103:7607-7612.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 56
    • 0031853099 scopus 로고    scopus 로고
    • Substrate and site specificity of hydrogen peroxide generation in mouse mitochondria
    • Kwong L.K., Sohal R.S. Substrate and site specificity of hydrogen peroxide generation in mouse mitochondria. Arch. Biochem. Biophys. 1998, 350:118-126.
    • (1998) Arch. Biochem. Biophys. , vol.350 , pp. 118-126
    • Kwong, L.K.1    Sohal, R.S.2
  • 57
    • 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., Brand M.D. Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 2004, 279:39414-39420.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 58
    • 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., Brand M.D. Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem. J. 2004, 382:511-517.
    • (2004) Biochem. J. , vol.382 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2
  • 60
    • 43049141441 scopus 로고    scopus 로고
    • Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport
    • Lambert A.J., Buckingham J.A., Boysen H.M., Brand M.D. Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport. Biochim. Biophys. Acta 2008, 1777:397-403.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 397-403
    • Lambert, A.J.1    Buckingham, J.A.2    Boysen, H.M.3    Brand, M.D.4
  • 61
    • 43549110469 scopus 로고    scopus 로고
    • Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state
    • Lambert A.J., Buckingham J.A., Brand M.D. Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state. FEBS Lett. 2008, 582:1711-1714.
    • (2008) FEBS Lett. , vol.582 , pp. 1711-1714
    • Lambert, A.J.1    Buckingham, J.A.2    Brand, M.D.3
  • 63
    • 0037228016 scopus 로고    scopus 로고
    • A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity
    • Lee S.S., Lee R.Y., Fraser A.G., Kamath R.S., Ahringer J., Ruvkun G. A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity. Nat. Genet. 2003, 33:40-48.
    • (2003) Nat. Genet. , vol.33 , pp. 40-48
    • Lee, S.S.1    Lee, R.Y.2    Fraser, A.G.3    Kamath, R.S.4    Ahringer, J.5    Ruvkun, G.6
  • 64
    • 0032545445 scopus 로고    scopus 로고
    • Diphenyleneiodonium, an NAD(P)H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production
    • Li Y., Trush M.A. Diphenyleneiodonium, an NAD(P)H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production. Biochem. Biophys. Res. Commun. 1998, 253:295-299.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 295-299
    • Li, Y.1    Trush, M.A.2
  • 66
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • Li N., Ragheb K., Lawler G., Sturgis J., Rajwa B., Melendez J.A., Robinson J.P. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J. Biol. Chem. 2003, 278:8516-8525.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3    Sturgis, J.4    Rajwa, B.5    Melendez, J.A.6    Robinson, J.P.7
  • 67
    • 0030722043 scopus 로고    scopus 로고
    • Generating, partitioning, targeting and functioning of superoxide in mitochondria
    • Liu S.S. Generating, partitioning, targeting and functioning of superoxide in mitochondria. Biosci. Rep. 1997, 17:259-272.
    • (1997) Biosci. Rep. , vol.17 , pp. 259-272
    • Liu, S.S.1
  • 68
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Liu Y., Fiskum G., Schubert D. Generation of reactive oxygen species by the mitochondrial electron transport chain. J. Neurochem. 2002, 80:780-787.
    • (2002) J. Neurochem. , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 69
    • 0033858360 scopus 로고    scopus 로고
    • The contribution of mitochondrial respiratory complexes to the production of reactive oxygen species
    • McLennan H.R., Degli Esposti M. The contribution of mitochondrial respiratory complexes to the production of reactive oxygen species. J. Bioenerg. Biomembr. 2000, 32:153-162.
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 153-162
    • McLennan, H.R.1    Degli Esposti, M.2
  • 71
    • 0037044847 scopus 로고    scopus 로고
    • Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
    • Messner K.R., Imlay J.A. Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase. J. Biol. Chem. 2002, 277:42563-42571.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42563-42571
    • Messner, K.R.1    Imlay, J.A.2
  • 72
    • 24344508510 scopus 로고    scopus 로고
    • The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria
    • Miwa S., Brand M.D. The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria. Biochim. Biophys. Acta 2005, 1709:214-219.
    • (2005) Biochim. Biophys. Acta , vol.1709 , pp. 214-219
    • Miwa, S.1    Brand, M.D.2
  • 73
    • 0141526414 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide production by Drosophila mitochondria
    • Miwa S., St-Pierre J., Partridge L., Brand M.D. Superoxide and hydrogen peroxide production by Drosophila mitochondria. Free Radical Biol. Med. 2003, 35:938-948.
    • (2003) Free Radical Biol. Med. , vol.35 , pp. 938-948
    • Miwa, S.1    St-Pierre, J.2    Partridge, L.3    Brand, M.D.4
  • 74
    • 38349158077 scopus 로고    scopus 로고
    • Simultaneous detection of apoptosis and mitochondrial superoxide production in live cells by flow cytometry and confocal microscopy
    • Mukhopadhyay P., Rajesh M., Hasko G., Hawkins B.J., Madesh M., Pacher P. Simultaneous detection of apoptosis and mitochondrial superoxide production in live cells by flow cytometry and confocal microscopy. Nat. Protoc. 2007, 2:2295-2301.
    • (2007) Nat. Protoc. , vol.2 , pp. 2295-2301
    • Mukhopadhyay, P.1    Rajesh, M.2    Hasko, G.3    Hawkins, B.J.4    Madesh, M.5    Pacher, P.6
  • 75
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller F.L., Liu Y., Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 2004, 279:49064-49073.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 77
    • 38749087624 scopus 로고    scopus 로고
    • High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates
    • Muller F.L., Liu Y., Abdul-Ghani M.A., Lustgarten M.S., Bhattacharya A., Jang Y.C., Van Remmen H. High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates. Biochem. J. 2008, 409:491-499.
    • (2008) Biochem. J. , 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    Van Remmen, H.7
  • 78
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy M.P. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417:1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 81
    • 0037114173 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species regulate spatial profile of proinflammatory responses in lung venular capillaries
    • Parthasarathi K., Ichimura H., Quadri S., Issekutz A., Bhattacharya J. Mitochondrial reactive oxygen species regulate spatial profile of proinflammatory responses in lung venular capillaries. J. Immunol. 2002, 169:7078-7086.
    • (2002) J. Immunol. , vol.169 , pp. 7078-7086
    • Parthasarathi, K.1    Ichimura, H.2    Quadri, S.3    Issekutz, A.4    Bhattacharya, J.5
  • 82
  • 83
  • 84
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S., Robinson B.H. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem. Sci. 2000, 25:502-508.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 85
    • 0034661024 scopus 로고    scopus 로고
    • Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase
    • Raha S., McEachern G.E., Myint A.T., Robinson B.H. Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase. Free Radical Biol. Med. 2000, 29:170-180.
    • (2000) Free Radical Biol. Med. , vol.29 , pp. 170-180
    • Raha, S.1    McEachern, G.E.2    Myint, A.T.3    Robinson, B.H.4
  • 86
    • 0036062729 scopus 로고    scopus 로고
    • Succinate dehydrogenase and human diseases: new insights into a well-known enzyme
    • Rustin P., Munnich A., Rotig A. Succinate dehydrogenase and human diseases: new insights into a well-known enzyme. Eur. J. Hum. Genet. 2002, 10:289-291.
    • (2002) Eur. J. Hum. Genet. , vol.10 , pp. 289-291
    • Rustin, P.1    Munnich, A.2    Rotig, A.3
  • 87
    • 33646704229 scopus 로고    scopus 로고
    • Is the mitochondrial free radical theory of aging intact?
    • Sanz A., Pamplona R., Barja G. Is the mitochondrial free radical theory of aging intact?. Antioxid. Redox Signaling 2006, 8:582-599.
    • (2006) Antioxid. Redox Signaling , vol.8 , pp. 582-599
    • Sanz, A.1    Pamplona, R.2    Barja, G.3
  • 88
    • 0033967558 scopus 로고    scopus 로고
    • Increased mitochondrial superoxide generation in neurons from trisomy 16 mice: a model of Down's syndrome
    • Schuchmann S., Heinemann U. Increased mitochondrial superoxide generation in neurons from trisomy 16 mice: a model of Down's syndrome. Free Radical Biol. Med. 2000, 28:235-250.
    • (2000) Free Radical Biol. Med. , vol.28 , pp. 235-250
    • Schuchmann, S.1    Heinemann, U.2
  • 89
    • 0023387645 scopus 로고
    • Generation of hydrogen peroxide by brown adipose tissue mitochondria
    • Sekhar B.S., Kurup C.K., Ramasarma T. Generation of hydrogen peroxide by brown adipose tissue mitochondria. J. Bioenerg. Biomembr. 1987, 19:397-407.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 397-407
    • Sekhar, B.S.1    Kurup, C.K.2    Ramasarma, T.3
  • 90
    • 0035834789 scopus 로고    scopus 로고
    • A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans
    • Senoo-Matsuda N., Yasuda K., Tsuda M., Ohkubo T., Yoshimura S., Nakazawa H., Hartman P.S., Ishii N. A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans. J. Biol. Chem. 2001, 276:41553-41558.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41553-41558
    • Senoo-Matsuda, N.1    Yasuda, K.2    Tsuda, M.3    Ohkubo, T.4    Yoshimura, S.5    Nakazawa, H.6    Hartman, P.S.7    Ishii, N.8
  • 91
    • 0025362247 scopus 로고
    • Overexpression of Cu-Zn superoxide dismutase in Drosophila does not affect life-span
    • Seto N.O., Hayashi S., Tener G.M. Overexpression of Cu-Zn superoxide dismutase in Drosophila does not affect life-span. Proc. Natl. Acad. Sci. USA 1990, 87:4270-4274.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4270-4274
    • Seto, N.O.1    Hayashi, S.2    Tener, G.M.3
  • 92
    • 65649134767 scopus 로고    scopus 로고
    • Mitochondrial respiratory complex I: structure, function and implication in human diseases
    • Sharma L.K., Lu J., Bai Y. Mitochondrial respiratory complex I: structure, function and implication in human diseases. Curr. Med. Chem. 2009, 16:1266-1277.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 1266-1277
    • Sharma, L.K.1    Lu, J.2    Bai, Y.3
  • 94
    • 0036138662 scopus 로고    scopus 로고
    • Endogenous and endobiotic induced reactive oxygen species formation by isolated hepatocytes
    • Siraki A.G., Pourahmad J., Chan T.S., Khan S., O'Brien P.J. Endogenous and endobiotic induced reactive oxygen species formation by isolated hepatocytes. Free Radical Biol. Med. 2002, 32:2-10.
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 2-10
    • Siraki, A.G.1    Pourahmad, J.2    Chan, T.S.3    Khan, S.4    O'Brien, P.J.5
  • 95
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev V.P. Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q. Rev. Biophys. 1996, 29:169-202.
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 96
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • Sohal R.S., Weindruch R. Oxidative stress, caloric restriction, and aging. Science 1996, 273:59-63.
    • (1996) Science , vol.273 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 97
    • 37849053352 scopus 로고    scopus 로고
    • Diabetic cardiomyopathy in OVE26 mice shows mitochondrial ROS production and divergence between in vivo and in vitro contractility
    • Song Y., Du Y., Prabhu S.D., Epstein P.N. Diabetic cardiomyopathy in OVE26 mice shows mitochondrial ROS production and divergence between in vivo and in vitro contractility. Rev. Diabet. Stud. 2007, 4:159-168.
    • (2007) Rev. Diabet. Stud. , vol.4 , pp. 159-168
    • Song, Y.1    Du, Y.2    Prabhu, S.D.3    Epstein, P.N.4
  • 99
    • 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., Brand M.D. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 2002, 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
  • 100
    • 0035989388 scopus 로고    scopus 로고
    • Induced overexpression of mitochondrial Mn-superoxide dismutase extends the life span of adult Drosophila melanogaster
    • Sun J., Folk D., Bradley T.J., Tower J. Induced overexpression of mitochondrial Mn-superoxide dismutase extends the life span of adult Drosophila melanogaster. Genetics 2002, 161:661-672.
    • (2002) Genetics , vol.161 , pp. 661-672
    • Sun, J.1    Folk, D.2    Bradley, T.J.3    Tower, J.4
  • 101
    • 0346094388 scopus 로고    scopus 로고
    • Production of endogenous matrix superoxide from mitochondrial complex I leads to activation of uncoupling protein 3
    • Talbot D.A., Lambert A.J., Brand M.D. Production of endogenous matrix superoxide from mitochondrial complex I leads to activation of uncoupling protein 3. FEBS Lett. 2004, 556:111-115.
    • (2004) FEBS Lett. , vol.556 , pp. 111-115
    • Talbot, D.A.1    Lambert, A.J.2    Brand, M.D.3
  • 102
    • 4544226082 scopus 로고    scopus 로고
    • Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase
    • Tretter L., Adam-Vizi V. Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase. J. Neurosci. 2004, 24:7771-7778.
    • (2004) J. Neurosci. , vol.24 , pp. 7771-7778
    • Tretter, L.1    Adam-Vizi, V.2
  • 104
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens J.F. Mitochondrial formation of reactive oxygen species. J. Physiol. 2003, 552:335-344.
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 105
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens J.F., Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 1980, 191:421-427.
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 106
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens J.F., Alexandre A., Lehninger A.L. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 1985, 237:408-414.
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 107
    • 0034740585 scopus 로고    scopus 로고
    • m-Dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • m-Dependent and -independent production of reactive oxygen species by rat brain mitochondria. J. Neurochem. 2001, 79:266-277.
    • (2001) J. Neurochem. , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 108
    • 0034903053 scopus 로고    scopus 로고
    • Altered mitochondrial function and overgeneration of reactive oxygen species precede the induction of apoptosis by 1-O-octadecyl-2-methyl-rac-glycero-3-phosphocholine in p53-defective hepatocytes
    • Vrablic A.S., Albright C.D., Craciunescu C.N., Salganik R.I., Zeisel S.H. Altered mitochondrial function and overgeneration of reactive oxygen species precede the induction of apoptosis by 1-O-octadecyl-2-methyl-rac-glycero-3-phosphocholine in p53-defective hepatocytes. FASEB J. 2001, 15:1739-1744.
    • (2001) FASEB J. , vol.15 , pp. 1739-1744
    • Vrablic, A.S.1    Albright, C.D.2    Craciunescu, C.N.3    Salganik, R.I.4    Zeisel, S.H.5
  • 109
    • 34548126843 scopus 로고    scopus 로고
    • Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: progress, pitfalls, and prospects
    • Wardman P. Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: progress, pitfalls, and prospects. Free Radical Biol. Med. 2007, 43:995-1022.
    • (2007) Free Radical Biol. Med. , vol.43 , pp. 995-1022
    • Wardman, P.1
  • 110
    • 42149117451 scopus 로고    scopus 로고
    • Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism
    • Yeh J.I., Chinte U., Du S. Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism. Proc. Natl. Acad. Sci. USA 2008, 105:3280-3285.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3280-3285
    • Yeh, J.I.1    Chinte, U.2    Du, S.3
  • 111
    • 0036718504 scopus 로고    scopus 로고
    • Reactive oxygen species production by the mitochondrial respiratory chain in isolated rat hepatocytes and liver mitochondria: studies using myxothiazol
    • Young T.A., Cunningham C.C., Bailey S.M. Reactive oxygen species production by the mitochondrial respiratory chain in isolated rat hepatocytes and liver mitochondria: studies using myxothiazol. Arch. Biochem. Biophys. 2002, 405:65-72.
    • (2002) Arch. Biochem. Biophys. , vol.405 , pp. 65-72
    • Young, T.A.1    Cunningham, C.C.2    Bailey, S.M.3


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