메뉴 건너뛰기




Volumn 456, Issue 3, 2013, Pages 441-452

The hydrogen-peroxide-induced radical behaviour in human cytochrome c-phospholipid complexes: Implications for the enhanced pro-apoptotic activity of the G41S mutant

Author keywords

Cardiolipin; Cytochrome c; Peroxidase; Phospholipid; Tyrosyl radical

Indexed keywords

CARDIOLIPIN; CYTOCHROME C; FREE RADICAL; HEME; HYDROGEN PEROXIDE; PEROXIDASE; PHOSPHOLIPID; TYROSINE;

EID: 84888402530     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130758     Document Type: Article
Times cited : (83)

References (50)
  • 1
    • 79953745644 scopus 로고    scopus 로고
    • The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis
    • Huttemann, M., Pecina, P., Rainbolt, M., Sanderson, T. H., Kagan, V. E., Samavati, L., Doan, J. W. and Lee, I. (2011) The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: from respiration to apoptosis. Mitochondrion 11, 369-381
    • (2011) Mitochondrion , vol.11 , pp. 369-381
    • Huttemann, M.1    Pecina, P.2    Rainbolt, M.3    Sanderson, T.H.4    Kagan, V.E.5    Samavati, L.6    Doan, J.W.7    Lee, I.8
  • 2
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu, X., Kim, C. N., Yang, J., Jemmerson, R. and Wang, X. (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86, 147-157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 3
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. (2001) The expanding role of mitochondria in apoptosis. Genes Dev. 15, 2922-2933
    • (2001) Genes Dev , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 5
    • 79551710218 scopus 로고    scopus 로고
    • The proapoptotic G41S mutation to human cytochrome c alters 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 c alters the heme electronic structure and increases the electron self-exchange rate. J. Am. Chem. Soc. 133, 1153-1155
    • (2011) 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.5
  • 6
    • 77951666026 scopus 로고    scopus 로고
    • Cytochrome c is rapidly reduced in the cytosol after mitochondrial outer membrane permeabilization
    • Ripple, M. O., Abajian, M. and Springett, R. (2010) Cytochrome c is rapidly reduced in the cytosol after mitochondrial outer membrane permeabilization. Apoptosis 15, 563-573
    • (2010) Apoptosis , vol.15 , pp. 563-573
    • Ripple, M.O.1    Abajian, M.2    Springett, R.3
  • 7
    • 35748954935 scopus 로고    scopus 로고
    • Mitochondrial regulation of caspase activation by cytochrome oxidase and tetramethylphenylenediamine via cytosolic cytochrome c redox state
    • Borutaite, V. and Brown, G. C. (2007) Mitochondrial regulation of caspase activation by cytochrome oxidase and tetramethylphenylenediamine via cytosolic cytochrome c redox state. J. Biol. Chem. 282, 31124-31130
    • (2007) J. Biol. Chem , vol.282 , pp. 31124-31130
    • Borutaite, V.1    Brown, G.C.2
  • 9
    • 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
    • (2000) Prog. Lipid Res , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 10
    • 83055197001 scopus 로고    scopus 로고
    • Probing a complex of cytochrome c and cardiolipin by magnetic circular dichroism spectroscopy: Implications for the initial events in apoptosis
    • Bradley, J. M., Silkstone, G., Wilson, M. T., Cheesman, M. R. and Butt, J. N. (2011) Probing a complex of cytochrome c and cardiolipin by magnetic circular dichroism spectroscopy: implications for the initial events in apoptosis. J. Am. Chem. Soc. 133, 19676-19679
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 19676-19679
    • Bradley, J.M.1    Silkstone, G.2    Wilson, M.T.3    Cheesman, M.R.4    Butt, J.N.5
  • 12
    • 0028836142 scopus 로고
    • Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions
    • Rytomaa, M. and Kinnunen, P. K. (1995) Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions. J. Biol. Chem. 270, 3197-3202
    • (1995) J. Biol. Chem , vol.270 , pp. 3197-3202
    • Rytomaa, M.1    Kinnunen, P.K.2
  • 13
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction: Evidence for the extended lipid anchorage
    • Tuominen, E. K., Wallace, C. J. and Kinnunen, P. K. (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.1    Wallace, C.J.2    Kinnunen, P.K.3
  • 15
    • 84869442007 scopus 로고    scopus 로고
    • Origin of the conformational heterogeneity of cardiolipin-bound cytochrome c
    • Hong, Y., Muenzner, J., Grimm, S. K. and Pletneva, E. V. (2012) Origin of the conformational heterogeneity of cardiolipin-bound cytochrome c. J. Am. Chem. Soc. 134, 18713-18723
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 18713-18723
    • Hong, Y.1    Muenzner, J.2    Grimm, S.K.3    Pletneva, E.V.4
  • 16
    • 0033595780 scopus 로고    scopus 로고
    • Loss of molecular interaction between cytochrome c and cardiolipin due to lipid peroxidation
    • Shidoji, Y., Hayashi, K., Komura, S., Ohishi, N. and Yagi, K. (1999) Loss of molecular interaction between cytochrome c and cardiolipin due to lipid peroxidation. Biochem. Biophys. Res. Commun. 264, 343-347
    • (1999) Biochem. Biophys. Res. Commun , vol.264 , pp. 343-347
    • Shidoji, Y.1    Hayashi, K.2    Komura, S.3    Ohishi, N.4    Yagi, K.5
  • 18
    • 13844255406 scopus 로고    scopus 로고
    • Reaction of haem containing proteins and enzymes with hydroperoxides: The radical view
    • Svistunenko, D. A. (2005) Reaction of haem containing proteins and enzymes with hydroperoxides: the radical view. Biochim. Biophys. Acta 1707, 127-155
    • (2005) Biochim. Biophys. Acta , vol.1707 , pp. 127-155
    • Svistunenko, D.A.1
  • 20
    • 0034647673 scopus 로고    scopus 로고
    • Oxidative signaling pathway for externalization of plasma membrane phosphatidylserine during apoptosis
    • Kagan, V. E., Fabisiak, J. P., Shvedova, A. A., Tyurina, Y. Y., Tyurin, V. A., Schor, N. F. and Kawai, K. (2000) Oxidative signaling pathway for externalization of plasma membrane phosphatidylserine during apoptosis. FEBS Lett. 477, 1-7
    • (2000) FEBS Lett , vol.477 , pp. 1-7
    • Kagan, V.E.1    Fabisiak, J.P.2    Shvedova, A.A.3    Tyurina, Y.Y.4    Tyurin, V.A.5    Schor, N.F.6    Kawai, K.7
  • 22
    • 1242294395 scopus 로고    scopus 로고
    • Lipid antioxidant, etoposide, inhibits phosphatidylserine externalization and macrophage clearance of apoptotic cells by preventing phosphatidylserine oxidation
    • Tyurina, Y. Y., Serinkan, F. B., Tyurin, V. A., Kini, V., Yalowich, J. C., Schroit, A. J., Fadeel, B. and Kagan, V. E. (2004) Lipid antioxidant, etoposide, inhibits phosphatidylserine externalization and macrophage clearance of apoptotic cells by preventing phosphatidylserine oxidation. J. Biol. Chem. 279, 6056-6064
    • (2004) J. Biol. Chem , vol.279 , pp. 6056-6064
    • Tyurina, Y.Y.1    Serinkan, F.B.2    Tyurin, V.A.3    Kini, V.4    Yalowich, J.C.5    Schroit, A.J.6    Fadeel, B.7    Kagan, V.E.8
  • 23
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition
    • Pollock, W. B., Rosell, F. I., Twitchett, M. B., Dumont, M. E. and Mauk, A. G. (1998) Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry 37, 6124-6131
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.1    Rosell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 24
    • 0001267512 scopus 로고
    • The oxidation potential of the system potassium ferrocyanide-potassium ferricyanide at various ionic strengths
    • Kolthoff, I. and Tomsicek, W. (1934) The oxidation potential of the system potassium ferrocyanide-potassium ferricyanide at various ionic strengths. J. Phys. Chem. 39, 945-954
    • (1934) J. Phys. Chem , vol.39 , pp. 945-954
    • Kolthoff, I.1    Tomsicek, W.2
  • 25
    • 78650119268 scopus 로고    scopus 로고
    • Compound ES of dehaloperoxidase decays via two alternative pathways depending on the conformation of the distal histidine
    • Thompson, M. K., Franzen, S., Ghiladi, R. A., Reeder, B. J. and Svistunenko, D. A. (2010) Compound ES of dehaloperoxidase decays via two alternative pathways depending on the conformation of the distal histidine. J. Am. Chem. Soc. 132, 17501-17510
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 17501-17510
    • Thompson, M.K.1    Franzen, S.2    Ghiladi, R.A.3    Reeder, B.J.4    Svistunenko, D.A.5
  • 26
    • 33745212211 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in patients with severe sepsis: An EPR interrogation of individual respiratory chain components
    • Svistunenko, D. A., Davies, N., Brealey, D., Singer, M. and Cooper, C. E. (2006) Mitochondrial dysfunction in patients with severe sepsis: an EPR interrogation of individual respiratory chain components. Biochim. Biophys. Acta 1757, 262-272
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 262-272
    • Svistunenko, D.A.1    Davies, N.2    Brealey, D.3    Singer, M.4    Cooper, C.E.5
  • 28
    • 3042773983 scopus 로고    scopus 로고
    • A new method of identifying the site of tyrosyl radicals in proteins
    • Svistunenko, D. A. and Cooper, C. E. (2004) A new method of identifying the site of tyrosyl radicals in proteins. Biophys. J. 87, 582-595
    • (2004) Biophys. J , vol.87 , pp. 582-595
    • Svistunenko, D.A.1    Cooper, C.E.2
  • 29
    • 68349089099 scopus 로고    scopus 로고
    • Tyrosyl radicals in proteins: A comparison of empirical and density functional calculated EPR parameters
    • Svistunenko, D. A. and Jones, G. A. (2009) Tyrosyl radicals in proteins: a comparison of empirical and density functional calculated EPR parameters. Phys. Chem. Chem. Phys. 11, 6600-6613
    • (2009) Phys. Chem. Chem. Phys , vol.11 , pp. 6600-6613
    • Svistunenko, D.A.1    Jones, G.A.2
  • 37
    • 0016256727 scopus 로고
    • Alkaline isomerization of oxidized cytochrome c. Equilibrium and kinetic measurements
    • Davis, L. A., Schejter, A. and Hess, G. P. (1974) Alkaline isomerization of oxidized cytochrome c. Equilibrium and kinetic measurements. 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
  • 38
    • 0014027971 scopus 로고
    • On the elucidation of the pH dependence of the oxidation-reduction potential of cytochrome c at alkaline pH
    • Brandt, K. G., Parks, P. C., Czerlinski, G. H. and Hess, G. P. (1966) On the elucidation of the pH dependence of the oxidation-reduction potential of cytochrome c at alkaline pH. J. Biol. Chem. 241, 4180-4185
    • (1966) J. Biol. Chem , vol.241 , pp. 4180-4185
    • Brandt, K.G.1    Parks, P.C.2    Czerlinski, G.H.3    Hess, G.P.4
  • 39
    • 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. JBIC, J. Biol. Inorg. Chem. 18, 289-297
    • (2013) JBIC, 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.8
  • 40
    • 0019888571 scopus 로고
    • Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8Å and comparison with the ferrocytochrome structure
    • Takano, T. and Dickerson, R. E. (1981) Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8Å and comparison with the ferrocytochrome structure. J. Mol. Biol. 153, 95-115
    • (1981) J. Mol. Biol , vol.153 , pp. 95-115
    • Takano, T.1    Dickerson, R.E.2
  • 41
    • 0023260274 scopus 로고
    • Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c
    • Gadsby, P. M., Peterson, J., Foote, N., Greenwood, C. and Thomson, A. J. (1987) Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c. Biochem. J. 246, 43-54
    • (1987) Biochem. J , vol.246 , pp. 43-54
    • Gadsby, P.M.1    Peterson, J.2    Foote, N.3    Greenwood, C.4    Thomson, A.J.5
  • 42
    • 0024537169 scopus 로고
    • Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids
    • Tonge, P., Moore, G. R. and Wharton, C. W. (1989) Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids. Biochem. J. 258, 599-605
    • (1989) Biochem. J , vol.258 , pp. 599-605
    • Tonge, P.1    Moore, G.R.2    Wharton, C.W.3
  • 44
    • 0037195257 scopus 로고    scopus 로고
    • Peroxidase activity as a tool for studying the folding of c-type cytochromes
    • Diederix, R. E. M., 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.M.1    Ubbink, M.2    Canters, G.W.3
  • 45
    • 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. (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.2
  • 46
    • 17144421250 scopus 로고    scopus 로고
    • Analysis of cytosolic and lysosomal pH in apoptotic cells by flow cytometry
    • Nilsson, C., Kagedal, K., Johansson, U. and Ollinger, K. (2003) Analysis of cytosolic and lysosomal pH in apoptotic cells by flow cytometry. Methods Cell Sci. 25, 185-194
    • (2003) Methods Cell Sci , vol.25 , pp. 185-194
    • Nilsson, C.1    Kagedal, K.2    Johansson, U.3    Ollinger, K.4
  • 47
    • 84867550132 scopus 로고    scopus 로고
    • Nitric oxide binding to the cardiolipin complex of ferric cytochrome c
    • Silkstone, G., Kapetanaki, S. M., Husu, I., Vos, M. H. and Wilson, M. T. (2012) Nitric oxide binding to the cardiolipin complex of ferric cytochrome c. Biochemistry 51, 6760-6766
    • (2012) Biochemistry , vol.51 , pp. 6760-6766
    • Silkstone, G.1    Kapetanaki, S.M.2    Husu, I.3    Vos, M.H.4    Wilson, M.T.5
  • 48
    • 0029864259 scopus 로고    scopus 로고
    • An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: Methods to quantify all paramagnetic species observed in the reaction
    • Svistunenko, D. A., Patel, R. P. and Wilson, M. T. (1996) An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: methods to quantify all paramagnetic species observed in the reaction. Free Radical Res. 24, 269-280
    • (1996) Free Radical Res , vol.24 , pp. 269-280
    • Svistunenko, D.A.1    Patel, R.P.2    Wilson, M.T.3
  • 49
    • 84860875640 scopus 로고    scopus 로고
    • Engineering tyrosine-based electron flow pathways in proteins: The case of aplysia myoglobin
    • Reeder, B. J., Svistunenko, D. A., Cooper, C. E. and Wilson, M. T. (2012) Engineering tyrosine-based electron flow pathways in proteins: the case of aplysia myoglobin. J. Am. Chem. Soc. 134, 7741-7749
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 7741-7749
    • Reeder, B.J.1    Svistunenko, D.A.2    Cooper, C.E.3    Wilson, M.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.