메뉴 건너뛰기




Volumn 88, Issue 3, 2004, Pages 657-667

Endogenous mitochondrial oxidative stress: Neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice

Author keywords

Antioxidant; Mitochondria; Neurodegeneration; Oxidative stress; Proteomics; Superoxide dismutase

Indexed keywords

ACONITATE HYDRATASE; ANTIOXIDANT; CITRATE SYNTHASE; CYTOCHROME C OXIDASE; HYDROGEN PEROXIDE; MANGANESE SUPEROXIDE DISMUTASE; MITOCHONDRIAL PROTEIN; OXOGLUTARATE DEHYDROGENASE; PARAQUAT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RESPIRATORY COMPLEX 1; RESPIRATORY COMPLEX 2; RESPIRATORY COMPLEX 3; RESPIRATORY COMPLEX 5; SUPEROXIDE DISMUTASE; TRICARBOXYLIC ACID; UNCLASSIFIED DRUG;

EID: 0942298545     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.02195.x     Document Type: Article
Times cited : (175)

References (54)
  • 1
    • 0036805853 scopus 로고    scopus 로고
    • Cytopathies involving mitochondrial complex II
    • Ackrell B. A. (2002) Cytopathies involving mitochondrial complex II. Mol. Aspects Med. 23, 369-384.
    • (2002) Mol. Aspects Med. , vol.23 , pp. 369-384
    • Ackrell, B.A.1
  • 2
    • 0021194505 scopus 로고
    • Effect of iron deficiency on succinate- and NADH-ubiquinone oxidoreductases in skeletal muscle mitochondria
    • Ackrell B. A., Maguire J. J., Dallman P. R. and Kearney E. B. (1984) Effect of iron deficiency on succinate- and NADH-ubiquinone oxidoreductases in skeletal muscle mitochondria. J. Biol. Chem. 259, 10053-10059.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10053-10059
    • Ackrell, B.A.1    Maguire, J.J.2    Dallman, P.R.3    Kearney, E.B.4
  • 3
    • 0001005014 scopus 로고
    • Structure and function of succinate dehydrogenase and fumarate reductase
    • (Muller, F., ed.). CRC Press, Boca Raton
    • Ackrell B. A. C., Johnson M. K., Gunsalus R. P. and Cecchini G. (1992) Structure and function of succinate dehydrogenase and fumarate reductase, in Chemistry and Biochemistry of Flavoenzymes, Vol. III (Muller, F., ed.), pp. 230-297. CRC Press, Boca Raton.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 230-297
    • Ackrell, B.A.C.1    Johnson, M.K.2    Gunsalus, R.P.3    Cecchini, G.4
  • 4
    • 0031911994 scopus 로고    scopus 로고
    • Synthetic combined superoxide dismutase/catalase mimetics are protective as a delayed treatment in a rat stroke model: A key role for reactive oxygen species in ischemic brain injury
    • Baker K., Marcus C. B., Huffman K., Kruk H., Malfroy B. and Doctrow S. R. (1998) Synthetic combined superoxide dismutase/catalase mimetics are protective as a delayed treatment in a rat stroke model: a key role for reactive oxygen species in ischemic brain injury. J. Pharmacol. Exp. Ther. 284, 215-221.
    • (1998) J. Pharmacol. Exp. Ther. , vol.284 , pp. 215-221
    • Baker, K.1    Marcus, C.B.2    Huffman, K.3    Kruk, H.4    Malfroy, B.5    Doctrow, S.R.6
  • 6
    • 0034803010 scopus 로고    scopus 로고
    • Phenotypic dichotomy in mitochondrial complex II genetic disorders
    • Baysal B. E., Rubinstein W. S. and Taschner P. E. (2001) Phenotypic dichotomy in mitochondrial complex II genetic disorders. J. Mol. Med. 79, 495-503.
    • (2001) J. Mol. Med. , vol.79 , pp. 495-503
    • Baysal, B.E.1    Rubinstein, W.S.2    Taschner, P.E.3
  • 7
    • 0017399780 scopus 로고
    • Interrelations of reconstitution activity, reactions with electron acceptors, and iron -sulfur centers in succinate dehydrogenase
    • Beinert H., Ackrell B. A., Vinogradov A. D., Kearney E. B. and Singer T. P. (1977) Interrelations of reconstitution activity, reactions with electron acceptors, and iron -sulfur centers in succinate dehydrogenase. Arch. Biochem. Biophys. 182, 95-106.
    • (1977) Arch. Biochem. Biophys. , vol.182 , pp. 95-106
    • Beinert, H.1    Ackrell, B.A.2    Vinogradov, A.D.3    Kearney, E.B.4    Singer, T.P.5
  • 8
    • 0033840193 scopus 로고    scopus 로고
    • Late-onset optic atrophy, ataxia, and myopathy associated with a mutation of a complex II gene
    • Birch-Machin M. A., Taylor R. W., Cochran B., Ackrell B. A. and Turnbull D. M. (2000) Late-onset optic atrophy, ataxia, and myopathy associated with a mutation of a complex II gene. Ann. Neurol. 48, 330-335.
    • (2000) Ann. Neurol. , vol.48 , pp. 330-335
    • Birch-Machin, M.A.1    Taylor, R.W.2    Cochran, B.3    Ackrell, B.A.4    Turnbull, D.M.5
  • 9
    • 0021288856 scopus 로고
    • Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria
    • Boveris A. (1984) Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria. Methods Enzymol. 105, 429-435.
    • (1984) Methods Enzymol. , vol.105 , pp. 429-435
    • Boveris, A.1
  • 10
    • 0004174608 scopus 로고    scopus 로고
    • Mitochondria and oxidative stress in amytrophic lateral sclerosis
    • (Beal, M. F., Howell, N. and Bodis-Wollner, I., eds). Wiley-Liss, New York
    • Brown R. H. (1997) Mitochondria and oxidative stress in amytrophic lateral sclerosis, in Mitochondria and Free Radicals in Neurodegenerative Diseases (Beal, M. F., Howell, N. and Bodis-Wollner, I., eds), pp. 309-318. Wiley-Liss, New York.
    • (1997) Mitochondria and Free Radicals in Neurodegenerative Diseases , pp. 309-318
    • Brown, R.H.1
  • 11
    • 0017592018 scopus 로고
    • Polypeptides in the succinate-coenzyme Q reductase segment of the respiratory chain
    • Capaldi R. A., Sweetland J. and Merli A. (1977) Polypeptides in the succinate-coenzyme Q reductase segment of the respiratory chain. Biochemistry 16, 5707-5710.
    • (1977) Biochemistry , vol.16 , pp. 5707-5710
    • Capaldi, R.A.1    Sweetland, J.2    Merli, A.3
  • 12
    • 0015239949 scopus 로고
    • Adenosine triphosphatase from rat liver mitochondria. I. Purification, homogeneity, and physical properties
    • Catterall W. A. and Pedersen P. L. (1971) Adenosine triphosphatase from rat liver mitochondria. I. Purification, homogeneity, and physical properties. J. Biol. Chem. 246, 4987-4994.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4987-4994
    • Catterall, W.A.1    Pedersen, P.L.2
  • 13
    • 0033000269 scopus 로고    scopus 로고
    • Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: Inhibition of alpha-ketoglutarate dehydrogenase
    • Chinopoulos C., Tretter L. and Adam-Vizi V. (1999) Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: inhibition of alpha-ketoglutarate dehydrogenase. J. Neurochem. 73, 220-228.
    • (1999) J. Neurochem. , vol.73 , pp. 220-228
    • Chinopoulos, C.1    Tretter, L.2    Adam-Vizi, V.3
  • 14
    • 0015236377 scopus 로고
    • Succinate dehydrogenase. I. Purification, molecular properties, and substructure
    • Davis K. A. and Hatefi Y. (1971) Succinate dehydrogenase. I. Purification, molecular properties, and substructure. Biochemistry 10, 2509-2516.
    • (1971) Biochemistry , vol.10 , pp. 2509-2516
    • Davis, K.A.1    Hatefi, Y.2
  • 16
    • 0029894380 scopus 로고    scopus 로고
    • Integrated evaluation of central nervous system lesions: Stains for neurons, astrocytes, and microglia reveal the spatial and temporal features of MK-801-induced neuronal necrosis in the rat cerebral cortex
    • Fix A. S., Ross J. F., Stitzel S. R. and Switzer R. C. (1996) Integrated evaluation of central nervous system lesions: stains for neurons, astrocytes, and microglia reveal the spatial and temporal features of MK-801-induced neuronal necrosis in the rat cerebral cortex. Toxicol. Pathol. 24, 291-304.
    • (1996) Toxicol. Pathol. , vol.24 , pp. 291-304
    • Fix, A.S.1    Ross, J.F.2    Stitzel, S.R.3    Switzer, R.C.4
  • 17
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner P. R., Raineri I., Epstein L. B. and White C. W. (1995) Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270, 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
  • 19
    • 0037441389 scopus 로고    scopus 로고
    • Characterization and function of mitochondrial nitric-oxide synthase
    • Giulivi C. (2003) Characterization and function of mitochondrial nitric-oxide synthase. Free Radic. Biol. Med. 34, 397-408.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 397-408
    • Giulivi, C.1
  • 21
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • Higgins C. M., Jung C., Ding H. and Xu Z. (2002) Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J Neurosci. 22, RC215.
    • (2002) J. Neurosci. , vol.22
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 23
    • 0032506040 scopus 로고    scopus 로고
    • Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal
    • Humphries K. M. and Szweda L. I. (1998) Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal. Biochemistry 37, 15835-15841.
    • (1998) Biochemistry , vol.37 , pp. 15835-15841
    • Humphries, K.M.1    Szweda, L.I.2
  • 24
    • 0034714346 scopus 로고    scopus 로고
    • Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease
    • Jha N., Jurma O., Lalli G., Liu Y., Pettus E. H., Greenamyre J. T., Liu R. M., Forman H. J. and Andersen J. K. (2000) Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease. J. Biol. Chem. 275, 26096-26101.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26096-26101
    • Jha, N.1    Jurma, O.2    Lalli, G.3    Liu, Y.4    Pettus, E.H.5    Greenamyre, J.T.6    Liu, R.M.7    Forman, H.J.8    Andersen, J.K.9
  • 25
    • 0036830072 scopus 로고    scopus 로고
    • Mitochondrial electron transport chain complex dysfunction in a transgenic mouse model for amyotrophic lateral sclerosis
    • Jung C., Higgins C. M. and Xu Z. (2002) Mitochondrial electron transport chain complex dysfunction in a transgenic mouse model for amyotrophic lateral sclerosis. J. Neurochem. 83, 535-545.
    • (2002) J. Neurochem. , vol.83 , pp. 535-545
    • Jung, C.1    Higgins, C.M.2    Xu, Z.3
  • 26
    • 0035947221 scopus 로고    scopus 로고
    • Synthetic superoxide dismutase/catalase mimetics reduce oxidative stress and prolong survival in a mouse amyotrophic lateral sclerosis model
    • Jung C., Rong Y., Doctrow S., Baudry M., Malfroy B. and Xu Z. (2001) Synthetic superoxide dismutase/catalase mimetics reduce oxidative stress and prolong survival in a mouse amyotrophic lateral sclerosis model. Neurosci. Lett. 304, 157-160.
    • (2001) Neurosci. Lett. , vol.304 , pp. 157-160
    • Jung, C.1    Rong, Y.2    Doctrow, S.3    Baudry, M.4    Malfroy, B.5    Xu, Z.6
  • 28
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin
    • Koutnikova H., Campuzano V., Foury F., Dolle P., Cazzalini O. and Koenig M. (1997) Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat. Genet. 16, 345-351.
    • (1997) Nat. Genet. , vol.16 , pp. 345-351
    • Koutnikova, H.1    Campuzano, V.2    Foury, F.3    Dolle, P.4    Cazzalini, O.5    Koenig, M.6
  • 29
    • 0035138456 scopus 로고    scopus 로고
    • Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
    • LaVaute T., Smith S., Cooperman S., Iwai K., Land W., Meyron-Holtz E., Drake S. K., Miller G., Abu-Asab M., Tsokos M. et al. (2001) Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice. Nat. Genet. 27, 209-214.
    • (2001) Nat. Genet. , vol.27 , pp. 209-214
    • LaVaute, T.1    Smith, S.2    Cooperman, S.3    Iwai, K.4    Land, W.5    Meyron-Holtz, E.6    Drake, S.K.7    Miller, G.8    Abu-Asab, M.9    Tsokos, M.10
  • 31
    • 0038491473 scopus 로고    scopus 로고
    • Reversal of age-related learning deficits and brain oxidative stress in mice with superoxide dismutase/catalase mimetics
    • Liu R., Liu I. Y., Bi X., Thompson R. F., Doctrow S. R., Malfroy B. and Baudry M. (2003) Reversal of age-related learning deficits and brain oxidative stress in mice with superoxide dismutase/catalase mimetics. Proc. Natl. Acad. Sci. USA 100, 8526-8531.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8526-8531
    • Liu, R.1    Liu, I.Y.2    Bi, X.3    Thompson, R.F.4    Doctrow, S.R.5    Malfroy, B.6    Baudry, M.7
  • 32
    • 0031562673 scopus 로고    scopus 로고
    • Prevention and suppression of autoimmune encephalomyelitis by EUK-8, a synthetic catalytic scavenger of oxygen-reactive metabolites
    • Malfroy B., Doctrow S. R., Orr P. L., Tocco G., Fedoseyeva E. V. and Benichou G. (1997) Prevention and suppression of autoimmune encephalomyelitis by EUK-8, a synthetic catalytic scavenger of oxygen-reactive metabolites. Cell Immunol. 177, 62-68.
    • (1997) Cell Immunol. , vol.177 , pp. 62-68
    • Malfroy, B.1    Doctrow, S.R.2    Orr, P.L.3    Tocco, G.4    Fedoseyeva, E.V.5    Benichou, G.6
  • 33
    • 0026004832 scopus 로고
    • Inhibition of glutathione synthesis in the newborn rat: A model for endogenously produced oxidative stress
    • Martensson J., Jain A., Stole E., Frayer W., Auld P. A. and Meister A. (1991) Inhibition of glutathione synthesis in the newborn rat: a model for endogenously produced oxidative stress. Proc. Natl Acad. Sci. USA 88, 9360-9364.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9360-9364
    • Martensson, J.1    Jain, A.2    Stole, E.3    Frayer, W.4    Auld, P.A.5    Meister, A.6
  • 37
    • 0035503501 scopus 로고    scopus 로고
    • Lifespan extension and rescue of spongiform encephalopathy in superoxide dismutase 2 nullizygous mice treated with superoxide dismutase-catalase mimetics
    • Melov S., Doctrow S. R., Schneider J. A., Haberson J., Patel M., Coskun P. E., Huffman K., Wallace D. C. and Malfroy B. (2001) Lifespan extension and rescue of spongiform encephalopathy in superoxide dismutase 2 nullizygous mice treated with superoxide dismutase-catalase mimetics. J. Neurosci. 21, 8348-8353.
    • (2001) J. Neurosci. , vol.21 , pp. 8348-8353
    • Melov, S.1    Doctrow, S.R.2    Schneider, J.A.3    Haberson, J.4    Patel, M.5    Coskun, P.E.6    Huffman, K.7    Wallace, D.C.8    Malfroy, B.9
  • 38
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya E. M., Bowling A. C. and Beal M. F. (1994) Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J. Neurochem. 63, 2179-2184.
    • (1994) J. Neurochem. , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 39
    • 0033638546 scopus 로고    scopus 로고
    • Cell size and oxidative enzyme activity of different types of fibers in different regions of the rat plantaris and tibialis anterior muscles
    • Nakatani T., Nakashima T., Kita T., Hirofuji C., Itoh K., Itoh M. and Ishihara A. (2000) Cell size and oxidative enzyme activity of different types of fibers in different regions of the rat plantaris and tibialis anterior muscles. Jpn J. Physiol. 50, 413-418.
    • (2000) Jpn. J. Physiol. , vol.50 , pp. 413-418
    • Nakatani, T.1    Nakashima, T.2    Kita, T.3    Hirofuji, C.4    Itoh, K.5    Itoh, M.6    Ishihara, A.7
  • 40
    • 0035968183 scopus 로고    scopus 로고
    • Modulation of mitochondrial function by hydrogen peroxide
    • Nulton-Persson A. C. and Szweda L. I. (2001) Modulation of mitochondrial function by hydrogen peroxide. J. Biol. Chem. 276, 23357-23361.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23357-23361
    • Nulton-Persson, A.C.1    Szweda, L.I.2
  • 41
    • 0028132219 scopus 로고
    • Use of Amino-cupric-silver technique for the detection of early and semiacute neuronal degeneration caused by neurotoxicants, hypoxia and physical trauma
    • de Olmos J. S., Beltramino C. A. and de Olmos de Lorenzo S. (1994) Use of Amino-cupric-silver technique for the detection of early and semiacute neuronal degeneration caused by neurotoxicants, hypoxia and physical trauma. Neurotoxicol. Teratol. 16, 545-561.
    • (1994) Neurotoxicol. Teratol. , vol.16 , pp. 545-561
    • De Olmos, J.S.1    Beltramino, C.A.2    De Olmos De Lorenzo, S.3
  • 42
    • 0034853453 scopus 로고    scopus 로고
    • Attenuation of staurosporine-induced apoptosis, oxidative stress, and mitochondrial dysfunction by synthetic superoxide dismutase and catalase mimetics, in cultured cortical neurons
    • Pong K., Doctrow S. R., Huffman K., Adinolfi C. A. and Baudry M. (2001) Attenuation of staurosporine-induced apoptosis, oxidative stress, and mitochondrial dysfunction by synthetic superoxide dismutase and catalase mimetics, in cultured cortical neurons. Exp. Neurol. 171, 84-97.
    • (2001) Exp. Neurol. , vol.171 , pp. 84-97
    • Pong, K.1    Doctrow, S.R.2    Huffman, K.3    Adinolfi, C.A.4    Baudry, M.5
  • 44
    • 0028936222 scopus 로고
    • Ragged red fibers in normal aging and inflammatory myopathy
    • Rifai Z., Welle S., Kamp C. and Thornton C. A. (1995) Ragged red fibers in normal aging and inflammatory myopathy [see comments]. Ann. Neurol. 37, 24-29.
    • (1995) Ann. Neurol. , vol.37 , pp. 24-29
    • Rifai, Z.1    Welle, S.2    Kamp, C.3    Thornton, C.A.4
  • 45
    • 0033578309 scopus 로고    scopus 로고
    • EUK-134, a synthetic superoxide dismutase and catalase mimetic, prevents oxidative stress and attenuates kainate-induced neuropathology
    • Rong Y., Doctrow S. R., Tocco G. and Baudry M. (1999) EUK-134, a synthetic superoxide dismutase and catalase mimetic, prevents oxidative stress and attenuates kainate-induced neuropathology. Proc. Natl Acad. Sci. USA 96, 9897-9902.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9897-9902
    • Rong, Y.1    Doctrow, S.R.2    Tocco, G.3    Baudry, M.4
  • 47
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • Seo M. S., Kang S. W., Kim K., Baines I. C., Lee T. H. and Rhee S. G. (2000) Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J. Biol. Chem. 275, 20346-20354.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20346-20354
    • Seo, M.S.1    Kang, S.W.2    Kim, K.3    Baines, I.C.4    Lee, T.H.5    Rhee, S.G.6
  • 48
    • 0037103792 scopus 로고    scopus 로고
    • Oxidation of nitric oxide by oxomanganese-salen complexes: A new mechanism for cellular protection by superoxide dismutase/catalase mimetics
    • Sharpe M. A., Ollosson R., Stewart V. C. and Clark J. B. (2002) Oxidation of nitric oxide by oxomanganese-salen complexes: a new mechanism for cellular protection by superoxide dismutase/catalase mimetics. Biochem. J. 366, 97-107.
    • (2002) Biochem. J. , vol.366 , pp. 97-107
    • Sharpe, M.A.1    Ollosson, R.2    Stewart, V.C.3    Clark, J.B.4
  • 49
    • 0028229152 scopus 로고
    • Mitochondrial DNA diseases: Histological and cellular studies
    • Shoubridge E. A. (1994) Mitochondrial DNA diseases: histological and cellular studies. J. Bioenerg. Biomembr 26, 301-310.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 301-310
    • Shoubridge, E.A.1
  • 52
    • 0029964226 scopus 로고    scopus 로고
    • Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines
    • Trounce I. A., Kim Y. L., Jun A. S. and Wallace D. C. (1996) Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines. Methods Enzymol. 264, 484-509.
    • (1996) Methods Enzymol. , vol.264 , pp. 484-509
    • Trounce, I.A.1    Kim, Y.L.2    Jun, A.S.3    Wallace, D.C.4
  • 53
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens J. F., Alexandre A. and Lehninger A. L. (1985) Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237, 408-414.
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.