메뉴 건너뛰기




Volumn 1709, Issue 3, 2005, Pages 214-219

The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria

Author keywords

Complex III; Drosophila; Glycerol phosphate dehydrogenase; Mitochondria; Superoxide

Indexed keywords

ACONITATE HYDRATASE; ANTIMYCIN A1; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; HYDROGEN PEROXIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUPEROXIDE; SUPEROXIDE DISMUTASE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 24344508510     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2005.08.003     Document Type: Article
Times cited : (96)

References (46)
  • 1
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W. Dröge Free radicals in the physiological control of cell function Physiol. Rev. 82 2002 47 95
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Dröge, W.1
  • 3
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • R.S. Sohal, and R. Weindruch Oxidative stress, caloric restriction, and aging Science 273 1996 59 63
    • (1996) Science , vol.273 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 4
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of ageing matures
    • K.B. Beckman, and B.N. Ames The free radical theory of ageing matures Physiol. Rev. 78 1998 547 581
    • (1998) Physiol. Rev. , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 5
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • E. Cadenas, and K.J. Davies Mitochondrial free radical generation, oxidative stress, and aging Free Radic. Biol. Med. 29 2000 222 230
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 7
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • A. Boveris, and B. Chance The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen Biochem. J. 134 1973 707 716
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 8
    • 0015694375 scopus 로고
    • 2 formation: Relationship with energy conservation
    • 2 formation: relationship with energy conservation FEBS Lett. 33 1973 84 87
    • (1973) FEBS Lett. , vol.33 , pp. 84-87
    • Loschen, G.1    Azzi, A.2    Flohe, L.3
  • 9
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • A. Boveris, N. Oshino, and B. Chance The cellular production of hydrogen peroxide Biochem. J. 128 1972 617 630
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 10
    • 0030969868 scopus 로고    scopus 로고
    • Superoxide production by the mitochondrial respiratory chain
    • J.F. Turrens Superoxide production by the mitochondrial respiratory chain Biosci. Rep. 17 1997 3 8
    • (1997) Biosci. Rep. , vol.17 , pp. 3-8
    • Turrens, J.F.1
  • 11
    • 0016148483 scopus 로고
    • Superoxide radicals as precursors of mitochondrial hydrogen peroxide
    • G. Loschen, A. Azzi, C. Richter, and L. Flohe Superoxide radicals as precursors of mitochondrial hydrogen peroxide FEBS Lett. 42 1974 68 72
    • (1974) FEBS Lett. , vol.42 , pp. 68-72
    • Loschen, G.1    Azzi, A.2    Richter, C.3    Flohe, L.4
  • 12
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • A. Boveris, E. Cadenas, and A.O. Stoppani Role of ubiquinone in the mitochondrial generation of hydrogen peroxide Biochem. J. 156 1976 435 444
    • (1976) Biochem. J. , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.3
  • 14
    • 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
    • A. Herrero, and G. Barja Sites and mechanisms responsible for the low rate of free radical production of heart mitochondria in the long-lived pigeon Mech. Ageing Dev. 98 1997 95 111
    • (1997) Mech. Ageing Dev. , vol.98 , pp. 95-111
    • Herrero, A.1    Barja, G.2
  • 15
    • 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
    • G. Barja 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. 31 1999 347 366
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 347-366
    • Barja, G.1
  • 16
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • J. St-Pierre, A.J. Buckingham, S.J. Roebuck, and M.D. Brand Topology of superoxide production from different sites in the mitochondrial electron transport chain J. Biol. Chem. 277 2002 44784 44790
    • (2002) J. Biol. Chem. , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, A.J.2    Roebuck, S.J.3    Brand, M.D.4
  • 17
    • 0027235532 scopus 로고
    • Aging, cytochrome oxidase activity, and hydrogen peroxide release by mitochondria
    • R.S. Sohal Aging, cytochrome oxidase activity, and hydrogen peroxide release by mitochondria Free Radic. Biol. Med. 14 1993 583 588
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 583-588
    • Sohal, R.S.1
  • 18
    • 0036244950 scopus 로고    scopus 로고
    • Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide
    • Z. Drahota, S.K. Chowdhury, D. Floryk, T. Mracek, J. Wilhelm, H. Rauchova, G. Lenaz, and J. Houstek Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide J. Bioenerg. Biomembr. 34 2002 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
  • 19
    • 0141526414 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide production by Drosophila mitochondria
    • S. Miwa, J. St-Pierre, L. Partridge, and M.D. Brand Superoxide and hydrogen peroxide production by Drosophila mitochondria Free Radic. Biol. Med. 35 2003 938 948
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 938-948
    • Miwa, S.1    St-Pierre, J.2    Partridge, L.3    Brand, M.D.4
  • 20
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • E. Cadenas, A. Boveris, C.I. Ragan, and A.O. Stoppani Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria Arch. Biochem. Biophys. 180 1977 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
  • 21
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • J.F. Turrens, and A. Boveris Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria Biochem. J. 191 1980 421 427
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 22
    • 0034467677 scopus 로고    scopus 로고
    • Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria
    • A. Herrero, and G. Barja Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria J. Bioenerg. Biomembr. 32 2000 609 615
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 609-615
    • Herrero, A.1    Barja, G.2
  • 23
    • 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
    • M.L. Genova, B. Ventura, G. Giuliano, C. Bovina, G. Formiggini, G. Parenti Castelli, and G. Lenaz The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2 FEBS Lett. 505 2001 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
  • 24
    • 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 Biochem. J. 368 2002 545 553
    • (2002) Biochem. J. , vol.368 , pp. 545-553
    • Kushnareva, Y.1    Murphy, A.N.2    Andreyev, A.3
  • 25
    • 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 J. Neurochem. 80 2002 780 787
    • (2002) J. Neurochem. , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 26
    • 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 Mol. Pharmacol. 64 2003 1136 1144
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1136-1144
    • Han, D.1    Canali, R.2    Rettori, D.3    Kaplowitz, N.4
  • 27
    • 10344221083 scopus 로고    scopus 로고
    • Complex III Releases superoxide to both sides of the inner mitochondrial membrane
    • F.L. Muller, Y. Liu, and H. Van Remmen Complex III Releases superoxide to both sides of the inner mitochondrial membrane J. Biol. Chem. 279 2004 49064 49073
    • (2004) J. Biol. Chem. , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 28
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • J.F. Turrens, A. Alexandre, and A.L. Lehninger Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria Arch. Biochem. Biophys. 237 1985 408 414
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 29
    • 0034661024 scopus 로고    scopus 로고
    • Superoxides from mitochondrial complex III: The role of manganese superoxide dismutase
    • S. Raha, G.E. McEachern, A.T. Myint, and B.H. Robinson Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase Free Radic. Biol. Med. 29 2000 170 180
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 170-180
    • Raha, S.1    McEachern, G.E.2    Myint, A.T.3    Robinson, B.H.4
  • 34
    • 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 Lett. 54 1975 311 314
    • (1975) FEBS Lett. , vol.54 , pp. 311-314
    • Boveris, A.1    Cadenas, E.2
  • 35
    • 0035863011 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
    • D. Han, E. Williams, and E. Cadenas Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space Biochem. J. 353 2001 411 416
    • (2001) Biochem. J. , vol.353 , pp. 411-416
    • Han, D.1    Williams, E.2    Cadenas, E.3
  • 36
    • 0037458619 scopus 로고    scopus 로고
    • Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
    • D. Han, F. Antunes, R. Canali, D. Rettori, and E. Cadenas Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol J. Biol. Chem. 278 2003 5557 5563
    • (2003) J. Biol. Chem. , vol.278 , pp. 5557-5563
    • Han, D.1    Antunes, F.2    Canali, R.3    Rettori, D.4    Cadenas, E.5
  • 37
    • 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 Eur. J. Biochem. 13 1970 247 252
    • (1970) Eur. J. Biochem. , vol.13 , pp. 247-252
    • Klingenberg, M.1
  • 38
    • 0014911245 scopus 로고
    • Specificity and locale of the L-3-glycerophosphate-flavoprotein oxidoreductase of mitochondria isolated from the flight muscle of Sarcophaga barbata Thoms
    • J.F. Donnellan, M.D. Barker, J. Wood, and R.B. Beechey Specificity and locale of the L-3-glycerophosphate-flavoprotein oxidoreductase of mitochondria isolated from the flight muscle of Sarcophaga barbata Thoms Biochem. J. 120 1970 467 478
    • (1970) Biochem. J. , vol.120 , pp. 467-478
    • Donnellan, J.F.1    Barker, M.D.2    Wood, J.3    Beechey, R.B.4
  • 39
    • 0030044236 scopus 로고    scopus 로고
    • Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied
    • M.J. MacDonald, and L.J. Brown Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied Arch. Biochem. Biophys. 326 1996 79 84
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 79-84
    • MacDonald, M.J.1    Brown, L.J.2
  • 40
    • 0036121191 scopus 로고    scopus 로고
    • Aconitase: Sensitive target and measure of superoxide
    • P.R. Gardner Aconitase: sensitive target and measure of superoxide Methods Enzymol. 349 2002 9 23
    • (2002) Methods Enzymol. , vol.349 , pp. 9-23
    • Gardner, P.R.1
  • 41
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • P.R. Gardner, I. Raineri, L.B. Epstein, and C.W. White Superoxide radical and iron modulate aconitase activity in mammalian cells J. Biol. Chem. 270 1995 13399 13405
    • (1995) J. Biol. Chem. , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 42
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • P.R. Gardner, and I. Fridovich Superoxide sensitivity of the Escherichia coli aconitase J. Biol. Chem. 266 1991 19328 19333
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 43
    • 0014216603 scopus 로고
    • Mechanism of aconitase action: I. the hydrogen transfer reaction
    • I.A. Rose, and E.L. O'Connell Mechanism of aconitase action: I. The hydrogen transfer reaction J. Biol. Chem. 242 1967 1870 1879
    • (1967) J. Biol. Chem. , vol.242 , pp. 1870-1879
    • Rose, I.A.1    O'Connell, E.L.2
  • 44
    • 0017817712 scopus 로고
    • Effects of superoxide on the erythrocyte membrane
    • R.E. Lynch, and I. Fridovich Effects of superoxide on the erythrocyte membrane J. Biol. Chem. 253 1978 1838 1845
    • (1978) J. Biol. Chem. , vol.253 , pp. 1838-1845
    • Lynch, R.E.1    Fridovich, I.2
  • 46
    • 0034442070 scopus 로고    scopus 로고
    • The nature and mechanism of superoxide production by the electron transport chain: Its relevance to aging
    • F. Muller The nature and mechanism of superoxide production by the electron transport chain: its relevance to aging J. Am. Aging Assoc. 23 2000 227 253
    • (2000) J. Am. Aging Assoc. , vol.23 , pp. 227-253
    • Muller, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.