메뉴 건너뛰기




Volumn 48, Issue 7, 2009, Pages 1613-1619

Interaction of carbon monoxide with the apoptosis-inducing cytochrome c-cardiolipin complex

Author keywords

[No Author keywords available]

Indexed keywords

ACYL CHAINS; ANTI-APOPTOTIC EFFECTS; APOPTOSIS; CARDIOLIPIN; CO CONCENTRATIONS; CYTOCHROME C; GEMINATE REBINDING; GEMINATE RECOMBINATIONS; HIGH AFFINITIES; INDUCED DISSOCIATIONS; INITIAL STAGES; MITOCHONDRIAL CYTOCHROMES; NANOMOLAR; ORDER OF MAGNITUDES; PEROXIDASE ACTIVITIES; PICOSECOND; POSITIVE SURFACE CHARGES; PROTEIN CONFORMATIONS; RESPIRATORY ELECTRONS; SECOND-ORDER RATE CONSTANTS;

EID: 61749099621     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801817v     Document Type: Article
Times cited : (73)

References (44)
  • 2
    • 0025146477 scopus 로고
    • High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c
    • Louie, G. V., and Brayer, G. D. (1990) High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c. J. Mol. Biol. 214, 527-555.
    • (1990) J. Mol. Biol , vol.214 , pp. 527-555
    • Louie, G.V.1    Brayer, G.D.2
  • 7
    • 0018399751 scopus 로고
    • Asymmetric distribution of phospholipids in the inner membrane of beef-heart mitochondria
    • Krebs, J. J. R., Hauser, H., and Carafoli, E. (1979) Asymmetric distribution of phospholipids in the inner membrane of beef-heart mitochondria. J. Biol. Chem. 254, 5308-5316.
    • (1979) J. Biol. Chem , vol.254 , pp. 5308-5316
    • Krebs, J.J.R.1    Hauser, H.2    Carafoli, E.3
  • 8
    • 0021804591 scopus 로고
    • Lipids of mitochondria
    • Daum, G. (1985) Lipids of mitochondria. Biochim. Biophys. Acta 822, 1-42.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 1-42
    • Daum, G.1
  • 11
    • 0038381423 scopus 로고    scopus 로고
    • Nitrosy-lation of cytochrome c during apoptosis
    • Schonhoff, C. M., Gaston, B., and Mannick, J. B. (2003) Nitrosy-lation of cytochrome c during apoptosis. J. Biol. Chem. 278, 18265-18270.
    • (2003) J. Biol. Chem , vol.278 , pp. 18265-18270
    • Schonhoff, C.M.1    Gaston, B.2    Mannick, J.B.3
  • 12
    • 33751003546 scopus 로고    scopus 로고
    • CO-metal interaction: Vital signaling from a lethal gas
    • Boczkowski, J., Poderoso, J. J., and Motterlini, R. (2006) CO-metal interaction: vital signaling from a lethal gas. Trends Biochem. Sci. 31, 614-621.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 614-621
    • Boczkowski, J.1    Poderoso, J.J.2    Motterlini, R.3
  • 13
    • 33845640469 scopus 로고    scopus 로고
    • HO-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism
    • Converso, D. P., Taille, C., Carreras, M. C., Jaitovich, A., Poderoso, J. J., and Boczkowski, J. (2006) HO-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism. FASEB J. 20, 1236-1238.
    • (2006) FASEB J , vol.20 , pp. 1236-1238
    • Converso, D.P.1    Taille, C.2    Carreras, M.C.3    Jaitovich, A.4    Poderoso, J.J.5    Boczkowski, J.6
  • 14
    • 0016739147 scopus 로고
    • Ligand binding to ferrocytochrome c at high pH
    • Moore, T. A., Greenwood, C., and Wilson, M. T. (1975) Ligand binding to ferrocytochrome c at high pH. Biochem. J. 147, 335-341.
    • (1975) Biochem. J , vol.147 , pp. 335-341
    • Moore, T.A.1    Greenwood, C.2    Wilson, M.T.3
  • 15
    • 27744526322 scopus 로고    scopus 로고
    • Geminate carbon monoxide rebinding to a c-type haem
    • Silkstone, G., Jasaitis, A., Vos, M. H., and Wilson, M. T. (2005) Geminate carbon monoxide rebinding to a c-type haem. Dalton Trans. 21, 3489-3494.
    • (2005) Dalton Trans , vol.21 , pp. 3489-3494
    • Silkstone, G.1    Jasaitis, A.2    Vos, M.H.3    Wilson, M.T.4
  • 16
    • 33847261166 scopus 로고    scopus 로고
    • Ligand dynamics in an electron-transfer protein: Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c
    • Silkstone, G., Jasaitis, A., Wilson, M. T., and Vos, M. H. (2007) Ligand dynamics in an electron-transfer protein: picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c. J. Biol. Chem. 282, 1638-1649.
    • (2007) J. Biol. Chem , vol.282 , pp. 1638-1649
    • Silkstone, G.1    Jasaitis, A.2    Wilson, M.T.3    Vos, M.H.4
  • 17
    • 0027423090 scopus 로고
    • Acid-induced unfolding and refolding transitions of cytochrome c: A three-state mechanism in water and deuterium oxide
    • Goto, Y., Hagihara, Y., Hamada, D., Hoshino, M., and Nishii, I. (1993) Acid-induced unfolding and refolding transitions of cytochrome c: A three-state mechanism in water and deuterium oxide. Biochemistry 32, 11878-11885.
    • (1993) Biochemistry , vol.32 , pp. 11878-11885
    • Goto, Y.1    Hagihara, Y.2    Hamada, D.3    Hoshino, M.4    Nishii, I.5
  • 18
    • 0008344554 scopus 로고
    • Side reactions in the deoxygenation of dilute oxyhaemoglobin solutions by sodium dithionite
    • Dalziel, K., and O'Brien, J. R. (1957) Side reactions in the deoxygenation of dilute oxyhaemoglobin solutions by sodium dithionite. Biochem. J. 67, 119-124.
    • (1957) Biochem. J , vol.67 , pp. 119-124
    • Dalziel, K.1    O'Brien, J.R.2
  • 19
    • 0037054860 scopus 로고    scopus 로고
    • Production and characterisation of Met80X mutants of yeast iso-1-cytochrome c: Spectral, photochemical and binding studies on the ferrous derivatives
    • Silkstone, G., Stanway, G., Brzezinski, P., and Wilson, M. T. (2002) Production and characterisation of Met80X mutants of yeast iso-1-cytochrome c: Spectral, photochemical and binding studies on the ferrous derivatives. Biophys. Chem. 98, 65-77.
    • (2002) Biophys. Chem , vol.98 , pp. 65-77
    • Silkstone, G.1    Stanway, G.2    Brzezinski, P.3    Wilson, M.T.4
  • 20
    • 0015718124 scopus 로고
    • Properties of modified cytochromes. II. Ligand binding to reduced carboxymethyl cytochrome c
    • Wilson, M. T., Brunori, M., Rotilio, G.C., and Antonini, E. (1973) Properties of modified cytochromes. II. Ligand binding to reduced carboxymethyl cytochrome c. J. Biol. Chem. 248, 8162-8169.
    • (1973) J. Biol. Chem , vol.248 , pp. 8162-8169
    • Wilson, M.T.1    Brunori, M.2    Rotilio, G.C.3    Antonini, E.4
  • 21
    • 0027424781 scopus 로고
    • A heme c-peptide model system for the resonance Raman study of c-type cytochromes: Characterization of the solvent-dependence of peptide-histidine-heme interactions
    • Othman, S., Le Lirzin, A., and Desbois, A. (1993) A heme c-peptide model system for the resonance Raman study of c-type cytochromes: Characterization of the solvent-dependence of peptide-histidine-heme interactions. Biochemistry 32, 9781-9791.
    • (1993) Biochemistry , vol.32 , pp. 9781-9791
    • Othman, S.1    Le Lirzin, A.2    Desbois, A.3
  • 22
    • 33749525655 scopus 로고    scopus 로고
    • Heme coordination states of unfolded ferrous cytochrome c
    • Droghetti, E., Oellerich, S., Hildebrandt, P., and Smulevich, G (2006) Heme coordination states of unfolded ferrous cytochrome c. Biophys. J. 91, 3022-3031.
    • (2006) Biophys. J , vol.91 , pp. 3022-3031
    • Droghetti, E.1    Oellerich, S.2    Hildebrandt, P.3    Smulevich, G.4
  • 23
    • 0037133134 scopus 로고    scopus 로고
    • Six- to five-coordinate heme-nitrosyl conversion in cytochrome ć and its relevance to guanylate cyclase
    • Andrew, C. R., George, S. J., Lawson, D. M., and Eady, R. R. (2002) Six- to five-coordinate heme-nitrosyl conversion in cytochrome ć and its relevance to guanylate cyclase. Biochemistry 41, 2353-2360.
    • (2002) Biochemistry , vol.41 , pp. 2353-2360
    • Andrew, C.R.1    George, S.J.2    Lawson, D.M.3    Eady, R.R.4
  • 24
    • 35048873629 scopus 로고    scopus 로고
    • Cytochrome c impaled: Investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models
    • Kalanxhi, E., and Wallace, C. J. A. (2007) Cytochrome c impaled: Investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models. Biochem. J. 407, 179-187.
    • (2007) Biochem. J , vol.407 , pp. 179-187
    • Kalanxhi, E.1    Wallace, C.J.A.2
  • 25
    • 0004224163 scopus 로고
    • Cevc, G, Ed, Marcel Dekker, New York
    • Cevc, G., Ed. (1993) Phospholipid Handbook, Marcel Dekker, New York.
    • (1993) Phospholipid Handbook
  • 26
    • 0024519403 scopus 로고
    • Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine
    • Springer, B. A., Egeberg, K. D., Sligar, S. G., Rohlfs, R. J., Mathews, A. J., and Olson, J. S. (1989) Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine. J. Biol. Chem. 264, 3057-3060.
    • (1989) J. Biol. Chem , vol.264 , pp. 3057-3060
    • Springer, B.A.1    Egeberg, K.D.2    Sligar, S.G.3    Rohlfs, R.J.4    Mathews, A.J.5    Olson, J.S.6
  • 27
    • 37549037456 scopus 로고    scopus 로고
    • Ultrafast dynamics of ligands within heme proteins
    • Vos, M. H. (2008) Ultrafast dynamics of ligands within heme proteins. Biochim. Biophys. Acta 1777, 15-31.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 15-31
    • Vos, M.H.1
  • 28
    • 0021757710 scopus 로고
    • Thermodynamic parameters for the reduction reaction of membrane-bound cytochrome-c in comparison with those of the membrane-free form: Spectropoten-tiostatic determination with use of an optically transparent thin-layer electrode
    • Huang, Y. Y., and Kimura, T. (1984) Thermodynamic parameters for the reduction reaction of membrane-bound cytochrome-c in comparison with those of the membrane-free form: Spectropoten-tiostatic determination with use of an optically transparent thin-layer electrode. Biochemistry 23, 2231-2236.
    • (1984) Biochemistry , vol.23 , pp. 2231-2236
    • Huang, Y.Y.1    Kimura, T.2
  • 29
    • 0037466114 scopus 로고    scopus 로고
    • Cytochrome c location in phosphatidylcholine/cardiolipin model membranes: Resonance energy transfer study
    • Gorbenko, G. P., and Domanov, Y. A. (2003) Cytochrome c location in phosphatidylcholine/cardiolipin model membranes: Resonance energy transfer study. Biophys. Chem. 103, 239-249.
    • (2003) Biophys. Chem , vol.103 , pp. 239-249
    • Gorbenko, G.P.1    Domanov, Y.A.2
  • 30
    • 33744942614 scopus 로고    scopus 로고
    • Cytochrome c interaction with cardiolipin/phosphatidylcholine model membranes: Effect of cardiolipin protonation
    • Gorbenko, G P., Molotkovsky, J. G., and Kinnunen, P. K. J. (2006) Cytochrome c interaction with cardiolipin/phosphatidylcholine model membranes: Effect of cardiolipin protonation. Biophys. J. 90, 4093-4103.
    • (2006) Biophys. J , vol.90 , pp. 4093-4103
    • Gorbenko, G.P.1    Molotkovsky, J.G.2    Kinnunen, P.K.J.3
  • 31
    • 27144462716 scopus 로고    scopus 로고
    • pH-dependent interaction of cytochrome c with mitochondrial mimetic membranes - The role of an array of positively charged amino acids
    • Kawai, C., Prado, F. M., Nunes, G. L. C., Di Mascio, P., Carmona-Ribeiro, A. M., and Nantes, I. L. (2005) pH-dependent interaction of cytochrome c with mitochondrial mimetic membranes - The role of an array of positively charged amino acids. J. Biol. Chem. 280, 34709-34717.
    • (2005) J. Biol. Chem , vol.280 , pp. 34709-34717
    • Kawai, C.1    Prado, F.M.2    Nunes, G.L.C.3    Di Mascio, P.4    Carmona-Ribeiro, A.M.5    Nantes, I.L.6
  • 32
    • 0039178090 scopus 로고    scopus 로고
    • Membrane location of spin-labeled cytochrome c determined by paramagnetic relaxation agents
    • Kostrzewa, A., Pali, T., Froncisz, W., and Marsh, D. (2000) Membrane location of spin-labeled cytochrome c determined by paramagnetic relaxation agents. Biochemistry 39, 6066-6074.
    • (2000) Biochemistry , vol.39 , pp. 6066-6074
    • Kostrzewa, A.1    Pali, T.2    Froncisz, W.3    Marsh, D.4
  • 34
    • 33846462466 scopus 로고    scopus 로고
    • A conformational switch to beta-sheet structure in cytochrome c leads to heme exposure. Implications for cardiolipin peroxidation and apoptosis
    • Balakrishnan, G., Hu, Y., Oyerinde, O. F., Su, J., Groves, J. T, and Spiro, T. G. (2007) A conformational switch to beta-sheet structure in cytochrome c leads to heme exposure. Implications for cardiolipin peroxidation and apoptosis. J. Am. Chem. Soc. 129, 504-505.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 504-505
    • Balakrishnan, G.1    Hu, Y.2    Oyerinde, O.F.3    Su, J.4    Groves, J.T.5    Spiro, T.G.6
  • 35
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction. Evidence for the extended lipid anchorage
    • Tuominen, E. K. J., Wallace, C. J. A., and Kinnunen, P. K. J. (2002) Phospholipid-cytochrome c interaction. Evidence for the extended lipid anchorage. J. Biol. Chem. 277, 8822-8826.
    • (2002) J. Biol. Chem , vol.277 , pp. 8822-8826
    • Tuominen, E.K.J.1    Wallace, C.J.A.2    Kinnunen, P.K.J.3
  • 39
    • 15944382742 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase
    • Ghafourifar, P., and Cadenas, E. (2005) Mitochondrial nitric oxide synthase. Trends Pharmacol. Sci. 26, 190-195.
    • (2005) Trends Pharmacol. Sci , vol.26 , pp. 190-195
    • Ghafourifar, P.1    Cadenas, E.2
  • 40
    • 0037124078 scopus 로고    scopus 로고
    • Heme oxygenase-1-derived carbon monoxide requires the activation of transcription factor NF-kappa B to protect endothelial cells from tumor necrosis factor-alpha-mediated apoptosis
    • Brouard, S., Berberat, P. O., Tobiasch, E., Seldon, M. P., Bach, F. H, and Soares, M. P. (2002) Heme oxygenase-1-derived carbon monoxide requires the activation of transcription factor NF-kappa B to protect endothelial cells from tumor necrosis factor-alpha-mediated apoptosis. J. Biol. Chem. 277, 17950-17961.
    • (2002) J. Biol. Chem , vol.277 , pp. 17950-17961
    • Brouard, S.1    Berberat, P.O.2    Tobiasch, E.3    Seldon, M.P.4    Bach, F.H.5    Soares, M.P.6
  • 41
    • 15744378615 scopus 로고    scopus 로고
    • Carbon monoxide differentially modulates STAT1 and STAT3 and inhibits apoptosis via a phosphatidylinositol 3-kinase/ Akt and p38 kinase-dependent STAT3 pathway during anoxia-reoxygenation injury
    • Zhang, X. C., Shan, P. Y., Alam, J., Fu, X. Y., and Lee, P. J. (2005) Carbon monoxide differentially modulates STAT1 and STAT3 and inhibits apoptosis via a phosphatidylinositol 3-kinase/ Akt and p38 kinase-dependent STAT3 pathway during anoxia-reoxygenation injury. J. Biol. Chem. 280, 8714-8721.
    • (2005) J. Biol. Chem , vol.280 , pp. 8714-8721
    • Zhang, X.C.1    Shan, P.Y.2    Alam, J.3    Fu, X.Y.4    Lee, P.J.5
  • 42
    • 0028955899 scopus 로고
    • Fast reactions of cytochrome oxidase
    • Einarsdottir, O. (1995) Fast reactions of cytochrome oxidase. Biochim. Biophys. Acta 1229, 129-147.
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 129-147
    • Einarsdottir, O.1
  • 43
    • 0036090811 scopus 로고    scopus 로고
    • Biological chemistry of carbon monoxide
    • Piantadosi, C. A. (2002) Biological chemistry of carbon monoxide. Antioxid. Redox Signal. 4, 259-270.
    • (2002) Antioxid. Redox Signal , vol.4 , pp. 259-270
    • Piantadosi, C.A.1
  • 44
    • 29844442868 scopus 로고    scopus 로고
    • Carbon monoxide: Endogenous production, physiological functions, and pharmacological applications
    • Wu, L., and Wang, R. (2005) Carbon monoxide: Endogenous production, physiological functions, and pharmacological applications. Pharmacol. Rev. 57, 585-630.
    • (2005) Pharmacol. Rev , vol.57 , pp. 585-630
    • Wu, L.1    Wang, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.