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Volumn 458, Issue 2, 2014, Pages 259-265

Enhancing the peroxidase activity of cytochrome c by mutation of residue 41: Implications for the peroxidase mechanism and cytochrome c release

Author keywords

Apoptosis; Cardiolipin; Cytochrome c; Mitochondrion; Omega loop; Peroxidase

Indexed keywords

ANIMALS; CYTOCHROMES C; ENZYME ACTIVATION; GENETIC VARIATION; HUMANS; MICE; MICE, INBRED C57BL; MICE, TRANSGENIC; MITOCHONDRIA, LIVER; MUTATION; PEROXIDASE; PROTEIN UNFOLDING;

EID: 84894238312     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20131386     Document Type: Article
Times cited : (37)

References (48)
  • 2
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • Riedl, S. J. and Salvesen, G. S. (2007) The apoptosome: signalling platform of cell death. Nat. Rev. Mol. Cell Biol. 8, 405-413
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 3
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome c-mediated apoptosis
    • Jiang, X. and Wang, X. (2004) Cytochrome c-mediated apoptosis. Annu. Rev. Biochem. 73, 87-106
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 87-106
    • Jiang, X.1    Wang, X.2
  • 5
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame, M., Rua, D. and Greenberg, M. L. (2000) The biosynthesis and functional role of cardiolipin. Prog. Lipid Res. 39, 257-288
    • Prog. Lipid Res. , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.L.3
  • 6
    • 0028836142 scopus 로고
    • Reversibility of the binding of cytochrome cto liposomes. Implications for lipid-protein interactions
    • Rytömaa, M. and Kinnunen, P. K. (1995) Reversibility of the binding of cytochrome cto liposomes. Implications for lipid-protein interactions. J. Biol. Chem. 270, 3197-3202
    • (1995) J. Biol. Chem. , vol.270 , pp. 3197-3202
    • Rytömaa, M.1    Kinnunen, P.K.2
  • 8
    • 0029900542 scopus 로고    scopus 로고
    • ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide
    • Barr, D. P., Gunther, M. R., Deterding, L. J., Tomer, K. B. and Mason, R. P. (1996) ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide. J. Biol. Chem. 271, 15498-15503
    • (1996) J. Biol. Chem. , vol.271 , pp. 15498-15503
    • Barr, D.P.1    Gunther, M.R.2    Deterding, L.J.3    Tomer, K.B.4    Mason, R.P.5
  • 9
    • 0023552833 scopus 로고
    • Free radicals in iron-containing systems
    • Dunford, H. B. (1987) Free radicals in iron-containing systems. Free Radic. Biol. Med. 3, 405-421
    • (1987) Free Radic. Biol. Med. , vol.3 , pp. 405-421
    • Dunford, H.B.1
  • 11
    • 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
  • 12
    • 77955010738 scopus 로고    scopus 로고
    • Misfolded proteins and neurodegeneration: Role of non-native cytochrome c in cell death
    • Santucci, R., Sinibaldi, F., Patriarca, A., Santucci, D. and Fiorucci, L. (2010) Misfolded proteins and neurodegeneration: role of non-native cytochrome c in cell death. Expert Rev. Proteomics 7, 507-517
    • (2010) Expert Rev. Proteomics , vol.7 , pp. 507-517
    • Santucci, R.1    Sinibaldi, F.2    Patriarca, A.3    Santucci, D.4    Fiorucci, L.5
  • 14
    • 0026498492 scopus 로고
    • Reversible, nonionic, and pH-dependent association of cytochrome cwith cardiolipin-phosphatidylcholine liposomes
    • Rytömaa, M., Mustonen, P. and Kinnunen, P. K. (1992) Reversible, nonionic, and pH-dependent association of cytochrome cwith cardiolipin- phosphatidylcholine liposomes. J. Biol. Chem. 267, 22243-22248
    • (1992) J. Biol. Chem. , vol.267 , pp. 22243-22248
    • Rytömaa, M.1    Mustonen, P.2    Kinnunen, P.K.3
  • 15
    • 35048873629 scopus 로고    scopus 로고
    • Cytochrome cimpaled: Investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models
    • Kalanxhi, E. and Wallace, C. J. A. (2007) Cytochrome cimpaled: 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
  • 16
    • 0028057721 scopus 로고
    • Evidence for two distinct acidic phospholipid-binding sites in cytochrome c
    • Rytömaa, M. and Kinnunen, P. K. (1994) Evidence for two distinct acidic phospholipid-binding sites in cytochrome c. J. Biol. Chem. 269, 1770-1774
    • (1994) J. Biol. Chem. , vol.269 , pp. 1770-1774
    • Rytömaa, M.1    Kinnunen, P.K.2
  • 18
    • 80053433149 scopus 로고    scopus 로고
    • Molecular mechanisms for the induction of peroxidase activity of the cytochrome c-cardiolipin complex
    • Abe, M., Niibayashi, R., Koubori, S., Moriyama, I. and Miyoshi, H. (2011) Molecular mechanisms for the induction of peroxidase activity of the cytochrome c-cardiolipin complex. Biochemistry 50, 8383-8391
    • (2011) Biochemistry , vol.50 , pp. 8383-8391
    • Abe, M.1    Niibayashi, R.2    Koubori, S.3    Moriyama, I.4    Miyoshi, H.5
  • 23
    • 79551710218 scopus 로고    scopus 로고
    • The proapoptotic G41S mutation to human cytochrome calters the heme electronic structure and increases the electron self-exchange rate
    • Liptak, M. D., Fagerlund, R. D., Ledgerwood, E. C., Wilbanks, S. M. and Bren, K. L. (2011) The proapoptotic G41S mutation to human cytochrome calters the heme electronic structure and increases the electron self-exchange rate. J. Am. Chem. Soc. 133, 1153-1155
    • J. Am. Chem. Soc. , vol.133 , pp. 1153-1155
    • Liptak, M.D.1    Fagerlund, R.D.2    Ledgerwood, E.C.3    Wilbanks, S.M.4    Bren, K.L.L.5
  • 24
    • 84878853376 scopus 로고    scopus 로고
    • Conformational change and human cytochrome c function: Mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination
    • Josephs, T. M., Liptak, M. D., Hughes, G., Lo, A., Smith, R. M., Wilbanks, S. M., Bren, K. L. and Ledgerwood, E. C. (2013) Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination. J. Biol. Inorg. Chem. 18, 289-297
    • J. Biol. Inorg. Chem. , vol.18 , pp. 289-297
    • Josephs, T.M.1    Liptak, M.D.2    Hughes, G.3    Lo, A.4    Smith, R.M.5    Wilbanks, S.M.6    Bren, K.L.7    Ledgerwood, E.C.C.8
  • 25
    • 84888402530 scopus 로고    scopus 로고
    • The hydrogen-peroxide-induced radical behaviour in human cytochrome c-phospholipid complexes: Implications for the enhanced pro-apoptotic activity of the G41S mutant
    • Rajagopal, B. S., Edzuma, A. N., Hough, M. A., Blundell, K. L., Kagan, V. E., Kapralov, A. A., Fraser, L. A., Butt, J. N., Silkstone, G. G., Wilson, M. T. et al. (2013) The hydrogen-peroxide-induced radical behaviour in human cytochrome c-phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant. Biochem. J. 456, 441-452
    • (2013) Biochem. J. , vol.456 , pp. 441-452
    • Rajagopal, B.S.1    Edzuma, A.N.2    Hough, M.A.3    Blundell, K.L.4    Kagan, V.E.5    Kapralov, A.A.6    Fraser, L.A.7    Butt, J.N.8    Silkstone, G.G.9    Wilson, M.T.10
  • 27
    • 0025821004 scopus 로고
    • Cytochrome c-catalyzed oxidation of organic molecules by hydrogen peroxide
    • Radi, R., Thomson, L., Rubbo, H. and Prodanov, E. (1991) Cytochrome c-catalyzed oxidation of organic molecules by hydrogen peroxide. Arch. Biochem. Biophys. 288, 112-117
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 112-117
    • Radi, R.1    Thomson, L.2    Rubbo, H.3    Prodanov, E.4
  • 30
    • 0030724539 scopus 로고    scopus 로고
    • Release of apoptogenic proteins from the mitochondrial intermembrane space during the mitochondrial permeability transition
    • Scarlett, J. L. and Murphy, M. P. (1997) Release of apoptogenic proteins from the mitochondrial intermembrane space during the mitochondrial permeability transition. FEBS Lett. 418, 282-286
    • (1997) FEBS Lett. , vol.418 , pp. 282-286
    • Scarlett, J.L.1    Murphy, M.P.2
  • 32
    • 0016256727 scopus 로고
    • Alkaline isomerization of oxidized cytochrome c
    • Davis, L. A., Schejter, A. and Hess, G. P. (1974) Alkaline isomerization of oxidized cytochrome c. J. Biol. Chem. 249, 2624-2632
    • (1974) J. Biol. Chem. , vol.249 , pp. 2624-2632
    • Davis, L.A.1    Schejter, A.2    Hess, G.P.3
  • 33
    • 33846462466 scopus 로고    scopus 로고
    • A conformational switch to β-sheet structure in cytochrome cleads 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 β-sheet structure in cytochrome cleads 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
  • 34
    • 10644280072 scopus 로고    scopus 로고
    • PH difference across the outer mitochondrial membrane measured with a green fluorescent protein mutant
    • Porcelli, A. M., Ghelli, A., Zanna, C., Pinton, P., Rizzuto, R. and Rugolo, M. (2005) pH difference across the outer mitochondrial membrane measured with a green fluorescent protein mutant. Biochem. Biophys. Res. Commun. 326, 799-804
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , pp. 799-804
    • Porcelli, A.M.1    Ghelli, A.2    Zanna, C.3    Pinton, P.4    Rizzuto, R.5    Rugolo, M.6
  • 35
    • 80053418385 scopus 로고    scopus 로고
    • Conformational stability of cytochrome cprobed by optical spectroscopy
    • Schweitzer-Stenner, R., Hagarman, A., Verbaro, D. and Soffer, J. B. (2009) Conformational stability of cytochrome cprobed by optical spectroscopy. Meth. Enzymol. 466, 109-153
    • (2009) Meth. Enzymol. , vol.466 , pp. 109-153
    • Schweitzer-Stenner, R.1    Hagarman, A.2    Verbaro, D.3    Soffer, J.B.4
  • 37
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein, J. C., Waterhouse, N. J., Juin, P., Evan, G. I. and Green, D. R. (2000) The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2, 156-162
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 38
    • 42149152141 scopus 로고    scopus 로고
    • Evaluating cytochrome cdiffusion in the intermembrane spaces of mitochondria during cytochrome crelease
    • Gillick, K. and Crompton, M. (2008) Evaluating cytochrome cdiffusion in the intermembrane spaces of mitochondria during cytochrome crelease. J. Cell Sci. 121, 618-626
    • (2008) J. Cell Sci. , vol.121 , pp. 618-626
    • Gillick, K.1    Crompton, M.2
  • 39
    • 0037016639 scopus 로고    scopus 로고
    • Effect of the protein matrix of cytochrome c in suppressing the inherent peroxidase activity of its heme prosthetic group
    • Diederix, R. E. M., Ubbink, M. and Canters, G. W. (2002) Effect of the protein matrix of cytochrome c in suppressing the inherent peroxidase activity of its heme prosthetic group. ChemBioChem 3, 110-112
    • (2002) ChemBioChem , vol.3 , pp. 110-112
    • Diederix, R.E.M.1    Ubbink, M.2    Canters, G.W.3
  • 40
    • 0038786579 scopus 로고    scopus 로고
    • Cooperative omega loops in cytochrome c: Role in folding and function
    • Krishna, M. M. G., Lin, Y., Rumbley, J. N. and Englander, S. W. (2003) Cooperative omega loops in cytochrome c: role in folding and function. J. Mol. Biol. 331, 29-36
    • (2003) J. Mol. Biol. , vol.331 , pp. 29-36
    • Krishna, M.M.G.1    Lin, Y.2    Rumbley, J.N.3    Englander, S.W.4
  • 41
    • 84869456778 scopus 로고    scopus 로고
    • His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: Implications for apoptosis
    • Balakrishnan, G., Hu, Y. and Spiro, T. G. (2012) His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis. J. Am. Chem. Soc. 134, 19061-19069
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 19061-19069
    • Balakrishnan, G.1    Hu, Y.2    Spiro, T.G.3
  • 42
    • 0033596909 scopus 로고    scopus 로고
    • A conformational change in cytochrome cof apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles
    • Jemmerson, R., Liu, J., Hausauer, D., Lam, K.-P., Mondino, A. and Nelson, R. D. (1999) A conformational change in cytochrome cof apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles. Biochemistry 38, 3599-3609
    • (1999) Biochemistry , vol.38 , pp. 3599-3609
    • Jemmerson, R.1    Liu, J.2    Hausauer, D.3    Lam, K.-P.4    Mondino, A.5    Nelson, R.D.6
  • 48
    • 81155155485 scopus 로고    scopus 로고
    • Nitration of tyrosines 46 and 48 induces the specific degradation of cytochrome cupon change of the heme iron state to high-spin
    • D́iaz-Moreno, I., Garćia-Heredia, J. M., D́iaz-Quintana, A., Teixeira, M. and De la Rosa, M. A. (2011) Nitration of tyrosines 46 and 48 induces the specific degradation of cytochrome cupon change of the heme iron state to high-spin. Biochim. Biophys. Acta 1807, 1616-1623
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1616-1623
    • D́iaz-Moreno, I.1    Garćia-Heredia, J.M.2    D́iaz-Quintana, A.3    Teixeira, M.4    De La Rosa, M.A.5


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