메뉴 건너뛰기




Volumn 9, Issue 1, 2010, Pages 78-91

Low complex I content explains the low hydrogen peroxide production rate of heart mitochondria from the long-lived pigeon, Columba livia

Author keywords

Comparative biology of aging; Complex I; Free radical theory of aging; Mitochondria; Reactive oxygen species; Superoxide

Indexed keywords

HYDROGEN PEROXIDE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINIC ACID; SUPEROXIDE DISMUTASE; ANTIOXIDANT; AVIAN PROTEIN;

EID: 76249116705     PISSN: 14749718     EISSN: 14749726     Source Type: Journal    
DOI: 10.1111/j.1474-9726.2009.00538.x     Document Type: Article
Times cited : (61)

References (89)
  • 2
    • 0036828726 scopus 로고    scopus 로고
    • Relative contributions of heart mitochondria glutathione peroxidase and catalase to H2O2 detoxification in in vivo conditions
    • Antunes F, Han D, Cadenas E. Relative contributions of heart mitochondria glutathione peroxidase and catalase to H2O2 detoxification in in vivo conditions. Free Radic. Biol. Med. 2002, 33:1260-1267.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1260-1267
    • Antunes, F.1    Han, D.2    Cadenas, E.3
  • 3
    • 0028955626 scopus 로고
    • 1-Chloro-2,4-dinitrobenzene is an irreversible inhibitor of human thioredoxin reductase. Loss of thioredoxin disulfide reductase activity is accompanied by a large increase in NADPH oxidase activity
    • Arner ES, Bjornstedt M, Holmgren A. 1-Chloro-2,4-dinitrobenzene is an irreversible inhibitor of human thioredoxin reductase. Loss of thioredoxin disulfide reductase activity is accompanied by a large increase in NADPH oxidase activity. J. Biol. Chem. 1995, 270:3479-3482.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3479-3482
    • Arner, E.S.1    Bjornstedt, M.2    Holmgren, A.3
  • 4
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban RS, Nemoto S, Finkel T. Mitochondria, oxidants, and aging. Cell 2005, 120:483-495.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 5
    • 0031721246 scopus 로고    scopus 로고
    • Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon
    • Barja G, Herrero A. Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon. J. Bioenerg. Biomembr. 1998, 30:235-243.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 235-243
    • Barja, G.1    Herrero, A.2
  • 6
    • 0033522924 scopus 로고    scopus 로고
    • Titrating the effects of mitochondrial complex I impairment in the cell physiology
    • Barrientos A, Moraes CT. 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
  • 7
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman KB, Ames BN. 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
  • 8
    • 78650998251 scopus 로고
    • The fluorometric measurement of the nucleotides of riboflavin and their concentration in tissues
    • Bessey OA, Lowry OH, Love RH. The fluorometric measurement of the nucleotides of riboflavin and their concentration in tissues. J. Biol. Chem. 1949, 180:755-769.
    • (1949) J. Biol. Chem. , vol.180 , pp. 755-769
    • Bessey, O.A.1    Lowry, O.H.2    Love, R.H.3
  • 9
    • 0016681098 scopus 로고
    • Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration
    • Boveris A, Cadenas E. Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration. FEBS Lett. 1975, 54:311-314.
    • (1975) FEBS Lett. , vol.54 , pp. 311-314
    • Boveris, A.1    Cadenas, E.2
  • 10
    • 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
  • 11
    • 0002114258 scopus 로고
    • Measurement of mitochondrial protonmotive force
    • Brown GC, Cooper CE. In, eds, Oxford, IRL Press, pp
    • Brand MD. Measurement of mitochondrial protonmotive force. Bioenergetics: A Practical Approach 1995, 39-62. Brown GCCooper CE. In, eds, Oxford, IRL Press, pp
    • (1995) Bioenergetics: A Practical Approach , pp. 39-62
    • Brand, M.D.1
  • 13
    • 0031898524 scopus 로고    scopus 로고
    • The proton permeability of the inner membrane of liver mitochondria from ectothermic and endothermic vertebrates and from obese rats: correlations with standard metabolic rate and phospholipid fatty acid composition
    • Brookes PS, Buckingham JA, Tenreiro AM, Hulbert AJ, Brand MD. The proton permeability of the inner membrane of liver mitochondria from ectothermic and endothermic vertebrates and from obese rats: correlations with standard metabolic rate and phospholipid fatty acid composition. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 1998, 119:325-334.
    • (1998) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.119 , pp. 325-334
    • Brookes, P.S.1    Buckingham, J.A.2    Tenreiro, A.M.3    Hulbert, A.J.4    Brand, M.D.5
  • 14
    • 37349000601 scopus 로고    scopus 로고
    • Correlation of mitochondrial superoxide dismutase and DNA polymerase beta in mammalian dermal fibroblasts with species maximal lifespan
    • Brown MF, Stuart JA. Correlation of mitochondrial superoxide dismutase and DNA polymerase beta in mammalian dermal fibroblasts with species maximal lifespan. Mech. Ageing Dev. 2007, 128:696-705.
    • (2007) Mech. Ageing Dev. , vol.128 , pp. 696-705
    • Brown, M.F.1    Stuart, J.A.2
  • 15
    • 0025007883 scopus 로고
    • Control of respiration and oxidative phosphorylation in isolated liver cells
    • Brown GC, Lakin-Thomas PL, Brand MD. Control of respiration and oxidative phosphorylation in isolated liver cells. Eur. J. Biochem. 1990, 192:355-362.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 355-362
    • Brown, G.C.1    Lakin-Thomas, P.L.2    Brand, M.D.3
  • 16
    • 0347359103 scopus 로고    scopus 로고
    • Reduced free-radical production and extreme longevity in the little brown bat (Myotis lucifugus) versus two non-flying mammals
    • Brunet-Rossinni AK. Reduced free-radical production and extreme longevity in the little brown bat (Myotis lucifugus) versus two non-flying mammals. Mech. Ageing Dev. 2004, 125:11-20.
    • (2004) Mech. Ageing Dev. , vol.125 , pp. 11-20
    • Brunet-Rossinni, A.K.1
  • 17
    • 0000631717 scopus 로고
    • Fluorimetric assay of FAD, FMN, and riboflavin
    • Burch HB. Fluorimetric assay of FAD, FMN, and riboflavin. Methods Enzymol. 1957, 3:960-962.
    • (1957) Methods Enzymol. , vol.3 , pp. 960-962
    • Burch, H.B.1
  • 18
    • 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 CI, Stoppani AO. 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
  • 19
    • 34249944839 scopus 로고    scopus 로고
    • A semiquinone intermediate generated at the Qo site of the cytochrome bc1 complex: importance for the Q-cycle and superoxide production
    • Cape JL, Bowman MK, Kramer DM. A semiquinone intermediate generated at the Qo site of the cytochrome bc1 complex: importance for the Q-cycle and superoxide production. Proc. Natl. Acad. Sci. U S A 2007, 104:7887-7892.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , pp. 7887-7892
    • Cape, J.L.1    Bowman, M.K.2    Kramer, D.M.3
  • 21
    • 0021777459 scopus 로고
    • Antioxidants and longevity of mammalian species
    • Cutler RG. Antioxidants and longevity of mammalian species. Basic Life Sci. 1985, 35:15-73.
    • (1985) Basic Life Sci. , vol.35 , pp. 15-73
    • Cutler, R.G.1
  • 23
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 2002, 82:47-95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 24
    • 0021288878 scopus 로고
    • Superoxide dismutase assays
    • Flohe L, Otting F. Superoxide dismutase assays. Methods Enzymol. 1984, 105:93-104.
    • (1984) Methods Enzymol. , vol.105 , pp. 93-104
    • Flohe, L.1    Otting, F.2
  • 25
    • 60249100683 scopus 로고    scopus 로고
    • Inverse relationship between longevity and evolutionary rate of mitochondrial proteins in mammals and birds
    • Galtier N, Blier PU, Nabholz B. Inverse relationship between longevity and evolutionary rate of mitochondrial proteins in mammals and birds. Mitochondrion. 2009, 9:51-57.
    • (2009) Mitochondrion. , vol.9 , pp. 51-57
    • Galtier, N.1    Blier, P.U.2    Nabholz, B.3
  • 26
    • 0042734428 scopus 로고    scopus 로고
    • Oxidative stress and aging: beyond correlation
    • Golden TR, Hinerfeld DA, 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
  • 27
    • 4744342460 scopus 로고    scopus 로고
    • Accelerated evolution of the electron transport chain in anthropoid primates
    • Grossman LI, Wildman DE, Schmidt TR, Goodman M. Accelerated evolution of the electron transport chain in anthropoid primates. Trends Genet. 2004, 20:578-585.
    • (2004) Trends Genet. , vol.20 , pp. 578-585
    • Grossman, L.I.1    Wildman, D.E.2    Schmidt, T.R.3    Goodman, M.4
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0030615104 scopus 로고    scopus 로고
    • Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age
    • Hansford RG, Hogue BA, Mildaziene V. Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age. J. Bioenerg. Biomembr. 1997, 29:89-95.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 89-95
    • Hansford, R.G.1    Hogue, B.A.2    Mildaziene, V.3
  • 31
    • 77049308856 scopus 로고
    • Aging: a theory based on free radical and radiation chemistry
    • Harman D. Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 1956, 11:298-300.
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 32
    • 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
  • 33
    • 0032525349 scopus 로고    scopus 로고
    • H2O2 production of heart mitochondria and aging rate are slower in canaries and parakeets than in mice: sites of free radical generation and mechanisms involved
    • Herrero A, Barja G. H2O2 production of heart mitochondria and aging rate are slower in canaries and parakeets than in mice: sites of free radical generation and mechanisms involved. Mech. Ageing Dev. 1998, 103:133-146.
    • (1998) Mech. Ageing Dev. , vol.103 , pp. 133-146
    • Herrero, A.1    Barja, G.2
  • 34
    • 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
  • 35
    • 53849099653 scopus 로고    scopus 로고
    • The production of reactive oxygen species by complex I
    • Hirst J, King MS, Pryde KR. 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
  • 36
    • 0023653390 scopus 로고
    • Respiratory control in the glucose perfused heart. A 31P NMR and NADH fluorescence study
    • Katz LA, Koretsky AP, Balaban RS. Respiratory control in the glucose perfused heart. A 31P NMR and NADH fluorescence study. FEBS Lett. 1987, 221:270-276.
    • (1987) FEBS Lett. , vol.221 , pp. 270-276
    • Katz, L.A.1    Koretsky, A.P.2    Balaban, R.S.3
  • 37
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov SS, Skulachev VP, Starkov AA. 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
  • 38
    • 0027517591 scopus 로고
    • Comparison of mitochondrial pro-oxidant generation and anti-oxidant defences between rat and pigeon: possible basis of variation in longevity and metabolic potential
    • Ku HH, Sohal RS. Comparison of mitochondrial pro-oxidant generation and anti-oxidant defences between rat and pigeon: possible basis of variation in longevity and metabolic potential. Mech. Ageing Dev. 1993, 72:67-76.
    • (1993) Mech. Ageing Dev. , vol.72 , pp. 67-76
    • Ku, H.H.1    Sohal, R.S.2
  • 39
    • 0027365312 scopus 로고
    • Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species
    • Ku HH, Brunk UT, Sohal RS. Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species. Free Radic. Biol. Med. 1993, 15:621-627.
    • (1993) Free Radic. Biol. Med. , vol.15 , pp. 621-627
    • Ku, H.H.1    Brunk, U.T.2    Sohal, R.S.3
  • 40
    • 0036903625 scopus 로고    scopus 로고
    • Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state
    • Kushnareva Y, Murphy AN, Andreyev A. Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state. Biochem. J. 2002, 368:545-553.
    • (2002) Biochem. J. , vol.368 , pp. 545-553
    • Kushnareva, Y.1    Murphy, A.N.2    Andreyev, A.3
  • 41
    • 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. U S A 2006, 103:7607-7612.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 42
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Lambert AJ, Brand MD. Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 2004a, 279:39414-39420.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 43
    • 4043090717 scopus 로고    scopus 로고
    • Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
    • Lambert AJ, Brand MD. Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem. J. 2004b, 382:511-517.
    • (2004) Biochem. J. , vol.382 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2
  • 45
    • 43549110469 scopus 로고    scopus 로고
    • Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state
    • Lambert AJ, Buckingham JA, Brand MD. Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state. FEBS Lett 2008a, 582:1711-1714.
    • (2008) FEBS Lett , vol.582 , pp. 1711-1714
    • Lambert, A.J.1    Buckingham, J.A.2    Brand, M.D.3
  • 46
    • 43049141441 scopus 로고    scopus 로고
    • Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport
    • Lambert AJ, Buckingham JA, Boysen HM, Brand MD. Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport. Biochim Biophys Acta 2008b, 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
  • 48
    • 42649123672 scopus 로고    scopus 로고
    • Do mitochondrial DNA and metabolic rate complement each other in determination of the mammalian maximum longevity?
    • Lehmann G, Segal E, Muradian KK, Fraifeld VE. Do mitochondrial DNA and metabolic rate complement each other in determination of the mammalian maximum longevity? Rejuvenation Res. 2008, 11:409-417.
    • (2008) Rejuvenation Res. , vol.11 , pp. 409-417
    • Lehmann, G.1    Segal, E.2    Muradian, K.K.3    Fraifeld, V.E.4
  • 49
    • 0032545445 scopus 로고    scopus 로고
    • Diphenyleneiodonium, an NAD(P)H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production
    • Li Y, Trush MA. 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
  • 51
    • 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 JA, Robinson JP. 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
  • 52
    • 0030722043 scopus 로고    scopus 로고
    • Generating, partitioning, targeting and functioning of superoxide in mitochondria
    • Liu SS. 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
  • 53
    • 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
  • 54
    • 0000466588 scopus 로고
    • Respiratory chain linked H(2)O(2) production in pigeon heart mitochondria
    • Loschen G, Flohe L, Chance B. Respiratory chain linked H(2)O(2) production in pigeon heart mitochondria. FEBS Lett. 1971, 18:261-264.
    • (1971) FEBS Lett. , vol.18 , pp. 261-264
    • Loschen, G.1    Flohe, L.2    Chance, B.3
  • 55
    • 0016148483 scopus 로고
    • Superoxide radicals as precursors of mitochondrial hydrogen peroxide
    • Loschen G, Azzi A, Richter C, Flohe L. Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS Lett. 1974, 42:68-72.
    • (1974) FEBS Lett. , vol.42 , pp. 68-72
    • Loschen, G.1    Azzi, A.2    Richter, C.3    Flohe, L.4
  • 56
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 1969, 244:6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 57
    • 38349126762 scopus 로고    scopus 로고
    • Mitochondrially encoded cysteine predicts animal lifespan
    • Moosmann B, Behl C. Mitochondrially encoded cysteine predicts animal lifespan. Aging Cell. 2008, 7:32-46.
    • (2008) Aging Cell. , vol.7 , pp. 32-46
    • Moosmann, B.1    Behl, C.2
  • 58
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller FL, 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
  • 60
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417:1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 62
    • 0036024975 scopus 로고    scopus 로고
    • Blue native electrophoresis to study mitochondrial and other protein complexes
    • Nijtmans LG, Henderson NS, Holt IJ. Blue native electrophoresis to study mitochondrial and other protein complexes. Methods. 2002, 26:327-334.
    • (2002) Methods. , vol.26 , pp. 327-334
    • Nijtmans, L.G.1    Henderson, N.S.2    Holt, I.J.3
  • 64
    • 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
  • 66
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S, Robinson BH. 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
  • 67
    • 33746919988 scopus 로고    scopus 로고
    • Longevity and the evolution of the mitochondrial DNA-coded proteins in mammals
    • Rottenberg H. Longevity and the evolution of the mitochondrial DNA-coded proteins in mammals. Mech. Ageing Dev. 2006, 127:748-760.
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 748-760
    • Rottenberg, H.1
  • 68
    • 33847619236 scopus 로고    scopus 로고
    • Coevolution of exceptional longevity, exceptionally high metabolic rates, and mitochondrial DNA-coded proteins in mammals
    • Rottenberg H. Coevolution of exceptional longevity, exceptionally high metabolic rates, and mitochondrial DNA-coded proteins in mammals. Exp. Gerontol. 2007, 42:364-373.
    • (2007) Exp. Gerontol. , vol.42 , pp. 364-373
    • Rottenberg, H.1
  • 70
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov LA, Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 2006, 311:1430-1436.
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 71
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H, von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 1991, 199:223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 72
    • 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 Radic. Biol. Med. 2000, 28:235-250.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 235-250
    • Schuchmann, S.1    Heinemann, U.2
  • 74
    • 0036138662 scopus 로고    scopus 로고
    • Endogenous and endobiotic induced reactive oxygen species formation by isolated hepatocytes
    • Siraki AG, Pourahmad J, Chan TS, Khan S, O'Brien PJ. Endogenous and endobiotic induced reactive oxygen species formation by isolated hepatocytes. Free Radic. Biol. Med. 2002, 32:2-10.
    • (2002) Free Radic. 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
  • 75
    • 0025363588 scopus 로고
    • Hydrogen peroxide production by liver mitochondria in different species
    • Sohal RS, Svensson I, Brunk UT. Hydrogen peroxide production by liver mitochondria in different species. Mech. Ageing Dev. 1990, 53:209-215.
    • (1990) Mech. Ageing Dev. , vol.53 , pp. 209-215
    • Sohal, R.S.1    Svensson, I.2    Brunk, U.T.3
  • 76
    • 0027442218 scopus 로고
    • Biochemical correlates of longevity in two closely related rodent species
    • Sohal RS, Ku HH, Agarwal S. Biochemical correlates of longevity in two closely related rodent species. Biochem. Biophys. Res. Commun. 1993, 196:7-11.
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 7-11
    • Sohal, R.S.1    Ku, H.H.2    Agarwal, S.3
  • 78
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre J, Buckingham JA, Roebuck SJ, Brand MD. 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
  • 79
    • 33845451992 scopus 로고    scopus 로고
    • The effect of bovine serum albumin on the membrane potential and reactive oxygen species generation in succinate-supported isolated brain mitochondria
    • Tretter L, Mayer-Takacs D, Adam-Vizi V. The effect of bovine serum albumin on the membrane potential and reactive oxygen species generation in succinate-supported isolated brain mitochondria. Neurochem. Int. 2007, 50:139-147.
    • (2007) Neurochem. Int. , vol.50 , pp. 139-147
    • Tretter, L.1    Mayer-Takacs, D.2    Adam-Vizi, V.3
  • 80
    • 0030969868 scopus 로고    scopus 로고
    • Superoxide production by the mitochondrial respiratory chain
    • Turrens JF. Superoxide production by the mitochondrial respiratory chain. Biosci. Rep. 1997, 17:3-8.
    • (1997) Biosci. Rep. , vol.17 , pp. 3-8
    • Turrens, J.F.1
  • 81
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens JF. Mitochondrial formation of reactive oxygen species. J. Physiol. 2003, 552:335-344.
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 82
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens JF, 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
  • 83
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens JF, Alexandre A, Lehninger AL. 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
  • 84
    • 0002156536 scopus 로고
    • The preparation of heart mitochondria from laboratory animals
    • Tyler DD, Gonze J. The preparation of heart mitochondria from laboratory animals. Methods Enzymol. 1967, 10:75-77.
    • (1967) Methods Enzymol. , vol.10 , pp. 75-77
    • Tyler, D.D.1    Gonze, J.2
  • 86
    • 0034740585 scopus 로고    scopus 로고
    • Δm-dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • Votyakova TV, Reynolds IJ. Δm-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
  • 87
    • 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 AS, Albright CD, Craciunescu CN, Salganik RI, Zeisel SH. 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
  • 88
  • 89
    • 34547850680 scopus 로고    scopus 로고
    • Succinate modulation of H2O2 release at NADH:ubiquinone oxidoreductase (complex I) in brain mitochondria
    • Zoccarato F, Cavallini L, Bortolami S, Alexandre A. Succinate modulation of H2O2 release at NADH:ubiquinone oxidoreductase (complex I) in brain mitochondria. Biochem. J. 2007, 406:125-129.
    • (2007) Biochem. J. , vol.406 , pp. 125-129
    • Zoccarato, F.1    Cavallini, L.2    Bortolami, S.3    Alexandre, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.