메뉴 건너뛰기




Volumn 46, Issue 11, 2007, Pages 3423-3434

Cardiolipin switch in mitochondria: Shutting off the reduction of cytochrome c and turning on the peroxidase activity

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CELL CULTURE; CELL MEMBRANES; CYCLIC VOLTAMMETRY; NEGATIVE IONS; OXIDATION; REDOX REACTIONS;

EID: 33947386195     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061854k     Document Type: Article
Times cited : (191)

References (64)
  • 4
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens, J. F. (2003) Mitochondrial formation of reactive oxygen species, J. Physiol. 552, 335-344.
    • (2003) J. Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 5
    • 33745591102 scopus 로고    scopus 로고
    • Multiple pathways of cytochrome c release from mitochondria in apoptosis
    • Gogvadze, V., Orrenius, S., and Zhivotovsky, B. (2006) Multiple pathways of cytochrome c release from mitochondria in apoptosis, Biochim. Biophys. Acta 1757, 639-647.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 639-647
    • Gogvadze, V.1    Orrenius, S.2    Zhivotovsky, B.3
  • 7
    • 28244442462 scopus 로고    scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in human disease
    • Fadeel, B., and Orrenius, S. (2005) Apoptosis: a basic biological phenomenon with wide-ranging implications in human disease, J. Intern. Med. 258, 479-517.
    • (2005) J. Intern. Med , vol.258 , pp. 479-517
    • Fadeel, B.1    Orrenius, S.2
  • 9
    • 26944463126 scopus 로고    scopus 로고
    • Phosphatidylserine-dependent engulfment by macrophages of nuclei from erythroid precursor cells
    • Yoshida, H., Kawane, K., Koike, M., Mori, Y., Uchiyama, Y., and Nagata, S. (2005) Phosphatidylserine-dependent engulfment by macrophages of nuclei from erythroid precursor cells, Nature 437, 754-758.
    • (2005) Nature , vol.437 , pp. 754-758
    • Yoshida, H.1    Kawane, K.2    Koike, M.3    Mori, Y.4    Uchiyama, Y.5    Nagata, S.6
  • 10
    • 0022520905 scopus 로고
    • Temperature dependence of the reduction potential of CuA in carbon monoxide inhibited cytochrome c oxidase
    • Wang, H., Blair, D. F., Ellis, W. R., Jr., Gray, H. B., and Chan, S. I. (1986) Temperature dependence of the reduction potential of CuA in carbon monoxide inhibited cytochrome c oxidase, Biochemistry 25, 167-171.
    • (1986) Biochemistry , vol.25 , pp. 167-171
    • Wang, H.1    Blair, D.F.2    Ellis Jr., W.R.3    Gray, H.B.4    Chan, S.I.5
  • 12
    • 0037195257 scopus 로고    scopus 로고
    • Peroxidase activity as a tool for studying the folding of c-type cytochromes
    • Diederix, R. E., Ubbink, M., and Canters, G. W. (2002) Peroxidase activity as a tool for studying the folding of c-type cytochromes, Biochemistry 41, 13067-13077.
    • (2002) Biochemistry , vol.41 , pp. 13067-13077
    • Diederix, R.E.1    Ubbink, M.2    Canters, G.W.3
  • 14
    • 0028080126 scopus 로고
    • The interaction of horse heart cytochrome c with phospholipid bilayers. Structural and dynamic effects
    • Pinheiro, T. J. (1994) The interaction of horse heart cytochrome c with phospholipid bilayers. Structural and dynamic effects, Biochimie 76, 489-500.
    • (1994) Biochimie , vol.76 , pp. 489-500
    • Pinheiro, T.J.1
  • 15
    • 0035808391 scopus 로고    scopus 로고
    • Effect of heme iron valence state on the conformation of cytochrome c and its association with membrane interfaces. A CD and EPR investigation
    • Nantes, I. L., Zucchi, M. R., Nascimento, O. R., and Faljoni-Alario, A. (2001) Effect of heme iron valence state on the conformation of cytochrome c and its association with membrane interfaces. A CD and EPR investigation, J. Biol. Chem. 276, 153-158.
    • (2001) J. Biol. Chem , vol.276 , pp. 153-158
    • Nantes, I.L.1    Zucchi, M.R.2    Nascimento, O.R.3    Faljoni-Alario, A.4
  • 16
    • 0015761138 scopus 로고
    • Correlations between structure and spectroscopic properties in membrane model system. Fluorescence and circular dichroism of the cytochrome c-cardiolipin system
    • Letellier, L., and Shechter, E. (1973) Correlations between structure and spectroscopic properties in membrane model system. Fluorescence and circular dichroism of the cytochrome c-cardiolipin system, Eur. J. Biochem. 40, 507-512.
    • (1973) Eur. J. Biochem , vol.40 , pp. 507-512
    • Letellier, L.1    Shechter, E.2
  • 17
    • 0034602452 scopus 로고    scopus 로고
    • Direct evidence for the cooperative unfolding of cytochrome c in lipid membranes from H-(2)H exchange kinetics
    • Pinheiro, T. J., Cheng, H., Seeholzer, S. H., and Roder, H. (2000) Direct evidence for the cooperative unfolding of cytochrome c in lipid membranes from H-(2)H exchange kinetics, J. Mol. Biol. 303, 617-626.
    • (2000) J. Mol. Biol , vol.303 , pp. 617-626
    • Pinheiro, T.J.1    Cheng, H.2    Seeholzer, S.H.3    Roder, H.4
  • 19
    • 0017374760 scopus 로고
    • NMR and ESR studies of the interactions of cytochrome c with mixed cardiolipin-phosphatidylcholine vesicles
    • Brown, L. R., and Wuthrich, K. (1977) NMR and ESR studies of the interactions of cytochrome c with mixed cardiolipin-phosphatidylcholine vesicles, Biochim. Biophys. Acta 468, 389-410.
    • (1977) Biochim. Biophys. Acta , vol.468 , pp. 389-410
    • Brown, L.R.1    Wuthrich, K.2
  • 20
    • 0025192083 scopus 로고
    • 1H-n.m.r. evaluation of the ferricytochrome c-cardiolipin interaction. Effect of superoxide radicals
    • 1H-n.m.r. evaluation of the ferricytochrome c-cardiolipin interaction. Effect of superoxide radicals, Biochem. J. 265, 227-232.
    • (1990) Biochem. J , vol.265 , pp. 227-232
    • Soussi, B.1    Bylund-Fellenius, A.C.2    Schersten, T.3    Angstrom, J.4
  • 21
    • 25444472873 scopus 로고    scopus 로고
    • Coverage-dependent changes of cytochrome c transverse location in phospholipid membranes revealed by FRET
    • Domanov, Y. A., Molotkovsky, J. G., and Gorbenko, G. P. (2005) Coverage-dependent changes of cytochrome c transverse location in phospholipid membranes revealed by FRET, Biochim. Biophys. Acta 1716, 49-58.
    • (2005) Biochim. Biophys. Acta , vol.1716 , pp. 49-58
    • Domanov, Y.A.1    Molotkovsky, J.G.2    Gorbenko, G.P.3
  • 22
    • 0030881010 scopus 로고    scopus 로고
    • Interaction of horse heart cytochrome c with lipid bilayer membranes: Effects on redox potentials
    • Salomon, Z., and Tollin, G. (1997) Interaction of horse heart cytochrome c with lipid bilayer membranes: effects on redox potentials, J. Bioenerg. Biomembr. 29, 211-221.
    • (1997) J. Bioenerg. Biomembr , vol.29 , pp. 211-221
    • Salomon, Z.1    Tollin, G.2
  • 23
    • 33748092382 scopus 로고    scopus 로고
    • Electrochemical and spectroscopic study on the interaction of cytochrome c with anionic lipid vesicles
    • Jing, W. G., Liu, C. W., Tang, J. L., Wu, Z. Y., Dong, S. J., and Wang, E. K. (2003) Electrochemical and spectroscopic study on the interaction of cytochrome c with anionic lipid vesicles, Chin. J. Chem. 21, 544-549.
    • (2003) Chin. J. Chem , vol.21 , pp. 544-549
    • Jing, W.G.1    Liu, C.W.2    Tang, J.L.3    Wu, Z.Y.4    Dong, S.J.5    Wang, E.K.6
  • 24
    • 0041810134 scopus 로고    scopus 로고
    • Redox and conformational equilibria and dynamics of cytochrome c at high electric fields
    • Wackerbarth, H., and Hildebrandt, P. (2003) Redox and conformational equilibria and dynamics of cytochrome c at high electric fields, ChemPhysChem. 4, 714-724.
    • (2003) ChemPhysChem , vol.4 , pp. 714-724
    • Wackerbarth, H.1    Hildebrandt, P.2
  • 25
    • 22444439802 scopus 로고    scopus 로고
    • Impact of surface immobilization and solution ionic strength on the formal potential of immobilized cytochrome c
    • Petrovic, J., Clark, R. A., Yue, H., Waldeck, D. H., and Bowden, E. F. (2005) Impact of surface immobilization and solution ionic strength on the formal potential of immobilized cytochrome c, Langmuir 21, 6308-6316.
    • (2005) Langmuir , vol.21 , pp. 6308-6316
    • Petrovic, J.1    Clark, R.A.2    Yue, H.3    Waldeck, D.H.4    Bowden, E.F.5
  • 28
    • 0030856714 scopus 로고    scopus 로고
    • Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide
    • Gudz, T. I., Tserng, K. Y., and Hoppel, C. L. (1997) Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide, J. Biol. Chem. 272, 24154-24158.
    • (1997) J. Biol. Chem , vol.272 , pp. 24154-24158
    • Gudz, T.I.1    Tserng, K.Y.2    Hoppel, C.L.3
  • 29
    • 0019804479 scopus 로고
    • Myxothiazol, a new inhibitor of the cytochrome b-c1 segment of the respiratory chain
    • Thierbach, G., and Reichenbach, H. (1981) Myxothiazol, a new inhibitor of the cytochrome b-c1 segment of the respiratory chain, Biochim. Biophys. Acta 638, 282-289.
    • (1981) Biochim. Biophys. Acta , vol.638 , pp. 282-289
    • Thierbach, G.1    Reichenbach, H.2
  • 30
    • 0028291367 scopus 로고
    • An evaluation of the measurement of the activities of complexes I-IV in the respiratory chain of human skeletal muscle mitochondria
    • Birch-Machin, M. A., Briggs, H. L., Saborido, A. A., Bindoff, L. A., and Turnbull, D. M. (1994) An evaluation of the measurement of the activities of complexes I-IV in the respiratory chain of human skeletal muscle mitochondria, Biochem. Med. Metab. Biol. 51, 35-42.
    • (1994) Biochem. Med. Metab. Biol , vol.51 , pp. 35-42
    • Birch-Machin, M.A.1    Briggs, H.L.2    Saborido, A.A.3    Bindoff, L.A.4    Turnbull, D.M.5
  • 31
    • 4444249485 scopus 로고    scopus 로고
    • High-performance liquid chromatography-based methods of enzymatic analysis: Electron transport chain activity in mitochondria from human skeletal muscle
    • Ritov, V. B., Menshikova, E. V., and Kelley, D. E. (2004) High-performance liquid chromatography-based methods of enzymatic analysis: electron transport chain activity in mitochondria from human skeletal muscle, Anal. Biochem. 333, 27-38.
    • (2004) Anal. Biochem , vol.333 , pp. 27-38
    • Ritov, V.B.1    Menshikova, E.V.2    Kelley, D.E.3
  • 33
    • 33947394653 scopus 로고    scopus 로고
    • Yonetani T. (1966) in Biochemical Preparations (Maehly, A. C., Ed.) pp 11, 14-20, John Wiley & Sons, New York.
    • Yonetani T. (1966) in Biochemical Preparations (Maehly, A. C., Ed.) pp 11, 14-20, John Wiley & Sons, New York.
  • 34
    • 0014410114 scopus 로고
    • The reduction of cytochrome c by milk xanthine oxidase
    • McCord, J. M., and Fridovich, I. (1968) The reduction of cytochrome c by milk xanthine oxidase, J. Biol. Chem. 243, 5753-5760.
    • (1968) J. Biol. Chem , vol.243 , pp. 5753-5760
    • McCord, J.M.1    Fridovich, I.2
  • 35
    • 0011666067 scopus 로고
    • Optically transparent thin layer electrode techniques for the study of biological redox systems
    • Heineman, W. R., Meckstroth, M. L., Norris, B. J., and Su, C.-Ho. (1979) Optically transparent thin layer electrode techniques for the study of biological redox systems, J. Electroanal. Chem. 104, 577-585.
    • (1979) J. Electroanal. Chem , vol.104 , pp. 577-585
    • Heineman, W.R.1    Meckstroth, M.L.2    Norris, B.J.3    Su, C.-H.4
  • 36
    • 0037077659 scopus 로고    scopus 로고
    • Direct wiring of cytochrome c's heme unit to an electrode: Electrochemical studies
    • Wei, J., Liu, H., Dick, A. R., Yamamoto, H., He, Y., and Waldeck, D. H. (2002) Direct wiring of cytochrome c's heme unit to an electrode: electrochemical studies, J. Am. Chem. Soc. 124, 9591-9599.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 9591-9599
    • Wei, J.1    Liu, H.2    Dick, A.R.3    Yamamoto, H.4    He, Y.5    Waldeck, D.H.6
  • 38
    • 33645502862 scopus 로고    scopus 로고
    • The effect of ionic strength on the electron-transfer rate of surface immobilized cytochrome c
    • Yue, H., Waldeck, D. H., Petrovic, J., and Clark, R. A. (2006) The effect of ionic strength on the electron-transfer rate of surface immobilized cytochrome c, J. Phys. Chem. B 110, 5062-5072.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 5062-5072
    • Yue, H.1    Waldeck, D.H.2    Petrovic, J.3    Clark, R.A.4
  • 39
    • 0035899737 scopus 로고    scopus 로고
    • The nature of electronic coupling between ferrocene and gold through alkanethiolate monolayers on electrodes: The importance of chain composition, interchain coupling, and quantum interference
    • Napper, A. M., Liu, H., and Waldeck, D. H. (2001) The nature of electronic coupling between ferrocene and gold through alkanethiolate monolayers on electrodes: the importance of chain composition, interchain coupling, and quantum interference, J. Phys. Chem. B 105, 7699-7707.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7699-7707
    • Napper, A.M.1    Liu, H.2    Waldeck, D.H.3
  • 40
    • 33748608019 scopus 로고    scopus 로고
    • Long-range electron-transfer reaction rates to cytochrome c across long- and short-chain alkanethiol self-assembled monolayers: Electroreflectance studies
    • Feng, Z. Q., Imabayashi, Sh., Kakiuchi, T., and Niki, K. (1997) Long-range electron-transfer reaction rates to cytochrome c across long- and short-chain alkanethiol self-assembled monolayers: Electroreflectance studies, J. Chem. Soc., Faraday Trans. 93, 1367-1370.
    • (1997) J. Chem. Soc., Faraday Trans , vol.93 , pp. 1367-1370
    • Feng, Z.Q.1    Imabayashi, S.2    Kakiuchi, T.3    Niki, K.4
  • 41
    • 0003998388 scopus 로고
    • Lide, D, Ed, /, 75th ed, p, CRC Press, Cleveland, OH
    • Lide, D., Ed. (1994/95) Handbook of Chemistry and Physics, 75th ed., p 965, CRC Press, Cleveland, OH.
    • (1994) Handbook of Chemistry and Physics , pp. 965
  • 42
    • 26444505495 scopus 로고    scopus 로고
    • Vitamin C enters mitochondria via facultative glucose transporter 1 (Glut1) and confers mitochondrial protection against oxidative injury
    • Sagun, K. C., Carcamo, J. M., and Golde, D. W. (2005) Vitamin C enters mitochondria via facultative glucose transporter 1 (Glut1) and confers mitochondrial protection against oxidative injury, FASEB J. 19, 1657-1667.
    • (2005) FASEB J , vol.19 , pp. 1657-1667
    • Sagun, K.C.1    Carcamo, J.M.2    Golde, D.W.3
  • 43
    • 0021236399 scopus 로고
    • Ascorbate reduction of horse heart cytochrome c. A zero-energy reduction reaction
    • Myer, Y. P., and Kumar, S. (1984) Ascorbate reduction of horse heart cytochrome c. A zero-energy reduction reaction, J. Biol. Chem. 259, 8144-8150.
    • (1984) J. Biol. Chem , vol.259 , pp. 8144-8150
    • Myer, Y.P.1    Kumar, S.2
  • 44
    • 33748638376 scopus 로고    scopus 로고
    • The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peroxyl or superoxide radicals in aqueous solutions in contact with oxygen
    • Petliki, J., and van de Ven, T. G. M. (1998) The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peroxyl or superoxide radicals in aqueous solutions in contact with oxygen, J. Chem. Soc., Faraday Trans. 94, 2763-2767.
    • (1998) J. Chem. Soc., Faraday Trans , vol.94 , pp. 2763-2767
    • Petliki, J.1    van de Ven, T.G.M.2
  • 45
    • 0020491099 scopus 로고
    • Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion
    • Butler, J., Koppenol, W. H., and Margoliash, E. (1982) Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion, J. Biol. Chem. 257, 10747-10750.
    • (1982) J. Biol. Chem , vol.257 , pp. 10747-10750
    • Butler, J.1    Koppenol, W.H.2    Margoliash, E.3
  • 46
    • 0035231595 scopus 로고    scopus 로고
    • Assaying mitochondrial respiratory complex activity in mitochondria isolated from human cells and tissues
    • Birch-Machin, M. A., and Turnbull, D. M. (2001) Assaying mitochondrial respiratory complex activity in mitochondria isolated from human cells and tissues, Methods Cell Biol. 65, 97-117.
    • (2001) Methods Cell Biol , vol.65 , pp. 97-117
    • Birch-Machin, M.A.1    Turnbull, D.M.2
  • 47
    • 0001325401 scopus 로고
    • The reduction of nitroso-spin traps in chemical and biological systems, a cautionary note
    • Kalyanaraman, B., Perez-Reyes, E., and Mason, R. P. (1979) The reduction of nitroso-spin traps in chemical and biological systems, a cautionary note, Tetrahedron Lett. 50, 4809-4812.
    • (1979) Tetrahedron Lett , vol.50 , pp. 4809-4812
    • Kalyanaraman, B.1    Perez-Reyes, E.2    Mason, R.P.3
  • 49
    • 0037101763 scopus 로고    scopus 로고
    • Mechanism in the reaction of cytochrome c oxidase with organic hydroperoxides: An ESR spin-trapping investigation
    • Chen, Y. R., and Mason, R. P. (2002) Mechanism in the reaction of cytochrome c oxidase with organic hydroperoxides: an ESR spin-trapping investigation, Biochem. J. 365, 461-469.
    • (2002) Biochem. J , vol.365 , pp. 461-469
    • Chen, Y.R.1    Mason, R.P.2
  • 50
    • 11144234843 scopus 로고    scopus 로고
    • 2+-induced reactive oxygen species production promotes cytochrome c release from rat liver mitochondria via mitochondrial permeability transition (MPT)-dependent and MPT-independent mechanisms: Role of cardiolipin
    • 2+-induced reactive oxygen species production promotes cytochrome c release from rat liver mitochondria via mitochondrial permeability transition (MPT)-dependent and MPT-independent mechanisms: role of cardiolipin, J. Biol. Chem. 279, 53103-53108.
    • (2004) J. Biol. Chem , vol.279 , pp. 53103-53108
    • Petrosillo, G.1    Ruggiero, F.M.2    Pistolese, M.3
  • 53
    • 23844540312 scopus 로고    scopus 로고
    • Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria
    • Zhang, M., Mileykovskaya, E., and Dowhan, W. (2005) Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria, J. Biol. Chem. 280, 29403-29408.
    • (2005) J. Biol. Chem , vol.280 , pp. 29403-29408
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 54
    • 0037113864 scopus 로고    scopus 로고
    • Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane
    • Zhang, M., Mileykovskaya, E., and Dowhan, W. (2002) Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane, J. Biol. Chem. 277, 43553-43556.
    • (2002) J. Biol. Chem , vol.277 , pp. 43553-43556
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 55
    • 4344561983 scopus 로고    scopus 로고
    • The mitochondrial respiratory chain is partially organized in a supercomplex assembly: Kinetic evidence using flux control analysis
    • Bianchi, C., Genova, M. L., Parenti, Castelli, G., and Lenaz, G. (2004) The mitochondrial respiratory chain is partially organized in a supercomplex assembly: kinetic evidence using flux control analysis, J. Biol. Chem. 279, 36562-36569.
    • (2004) J. Biol. Chem , vol.279 , pp. 36562-36569
    • Bianchi, C.1    Genova, M.2    Parenti, L.3    Castelli, G.4    Lenaz, G.5
  • 57
    • 0347481136 scopus 로고    scopus 로고
    • Transbilayer lipid diffusion promoted by Bax: Implications for apoptosis
    • Epand, R. F., Martinou, J.-C., Montessuit, S., and Epand, R. M. (2003) Transbilayer lipid diffusion promoted by Bax: implications for apoptosis, Biochemistry 42, 14576-14582
    • (2003) Biochemistry , vol.42 , pp. 14576-14582
    • Epand, R.F.1    Martinou, J.-C.2    Montessuit, S.3    Epand, R.M.4
  • 59
    • 13244251228 scopus 로고    scopus 로고
    • An epigrammatic (abridged) recounting of the myriad tales of astonishing deeds and dire consequences pertaining to nitric oxide and reactive oxygen species in mitochondria with an ancillary missive concerning the origins of apoptosis
    • Heck, D. E., Kagan, V. E., Shvedova, A. A., and Laskin, J. D. (2005) An epigrammatic (abridged) recounting of the myriad tales of astonishing deeds and dire consequences pertaining to nitric oxide and reactive oxygen species in mitochondria with an ancillary missive concerning the origins of apoptosis, Toxicology 208, 259-271.
    • (2005) Toxicology , vol.208 , pp. 259-271
    • Heck, D.E.1    Kagan, V.E.2    Shvedova, A.A.3    Laskin, J.D.4
  • 60
    • 2342417321 scopus 로고    scopus 로고
    • Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical
    • Chen, Y. R., Chen, C. L., Chen, W., Zweier, J. L., Augusta, O., Radi, R., and Mason, R. P. (2004) Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical, J. Biol. Chem. 279, 18054-18062.
    • (2004) J. Biol. Chem , vol.279 , pp. 18054-18062
    • Chen, Y.R.1    Chen, C.L.2    Chen, W.3    Zweier, J.L.4    Augusta, O.5    Radi, R.6    Mason, R.P.7
  • 62
    • 0035812628 scopus 로고    scopus 로고
    • Folding of horse cytochrome c in the reduced state
    • Bhuyan, A. K., and Udgaonkar, J. B. (2004) Folding of horse cytochrome c in the reduced state, J. Mol. Biol. 312, 1135-1160.
    • (2004) J. Mol. Biol , vol.312 , pp. 1135-1160
    • Bhuyan, A.K.1    Udgaonkar, J.B.2
  • 64
    • 18344405929 scopus 로고    scopus 로고
    • Generation of superoxide anion by mitochondria and impairment of their functions during anoxia and reoxygenation in vitro
    • Du, G., Mouithys-Mickalad, A., and Sluse, F. E. (1998) Generation of superoxide anion by mitochondria and impairment of their functions during anoxia and reoxygenation in vitro, Free Radical Biol. Med. 25, 1066-1074.
    • (1998) Free Radical Biol. Med , vol.25 , pp. 1066-1074
    • Du, G.1    Mouithys-Mickalad, A.2    Sluse, F.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.