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Volumn 404, Issue 1, 2011, Pages 190-194

Cardiolipin modulates allosterically peroxynitrite detoxification by horse heart cytochrome c

Author keywords

Allostery; Cardiolipin; Horse heart cytochrome c; Peroxynitrite isomerization

Indexed keywords

BOVINE HEART CARDIOLIPIN; CARDIOLIPIN; CYTOCHROME C; FERRIC CYTOCHROME C; HORSE HEART CYTOCHROME C; PEROXYNITRITE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 78650897503     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.11.091     Document Type: Article
Times cited : (31)

References (40)
  • 4
    • 70450205079 scopus 로고    scopus 로고
    • Apoptosis and human diseases: mitochondrion damage and lethal role of cytochrome c as proapoptotic protein
    • Caroppi P., Sinibaldi F., Fiorucci L., Santucci R. Apoptosis and human diseases: mitochondrion damage and lethal role of cytochrome c as proapoptotic protein. Curr. Med. Chem. 2009, 16:4058-4065.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 4058-4065
    • Caroppi, P.1    Sinibaldi, F.2    Fiorucci, L.3    Santucci, R.4
  • 6
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H., Li Y., Liu X., Wang X. An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 1999, 274:11549-11556.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 7
    • 0034710942 scopus 로고    scopus 로고
    • Cytochrome c binding to Apaf-1: the effects of dATP and ionic strength
    • Purring-Koch C., McLendon G. Cytochrome c binding to Apaf-1: the effects of dATP and ionic strength. Proc. Natl Acad. Sci. USA 2000, 97:11928-11931.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 11928-11931
    • Purring-Koch, C.1    McLendon, G.2
  • 8
    • 2442540299 scopus 로고    scopus 로고
    • Pro-apoptotic proteins released from the mitochondria regulate the protein composition and caspase-processing activity of the native Apaf-1/caspase-9 apoptosome complex
    • Twiddy D., Brown D.G., Adrain C., Jukes R., Martin S.J., Cohen G.M., MacFarlane M., Cain K. Pro-apoptotic proteins released from the mitochondria regulate the protein composition and caspase-processing activity of the native Apaf-1/caspase-9 apoptosome complex. J. Biol. Chem. 2004, 279:19665-19682.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19665-19682
    • Twiddy, D.1    Brown, D.G.2    Adrain, C.3    Jukes, R.4    Martin, S.J.5    Cohen, G.M.6    MacFarlane, M.7    Cain, K.8
  • 10
    • 70349551416 scopus 로고    scopus 로고
    • The physicochemical properties of cardiolipin bilayers and cardiolipin-containing lipid membranes
    • Lewis R.N., McElhaney R.N. The physicochemical properties of cardiolipin bilayers and cardiolipin-containing lipid membranes. Biochim. Biophys. Acta 2009, 1788:2069-2079.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2069-2079
    • Lewis, R.N.1    McElhaney, R.N.2
  • 12
    • 0028057721 scopus 로고
    • Evidence for two distinct acidic phospholipids-binding sites in cytochrome c
    • Rytömaa M., Kinnunen P.K.J. Evidence for two distinct acidic phospholipids-binding sites in cytochrome c. J. Biol. Chem. 1994, 269:1770-1774.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1770-1774
    • Rytömaa, M.1    Kinnunen, P.K.J.2
  • 13
    • 0028836142 scopus 로고
    • Reversibility of the binding of cytochrome c liposomes: implications for lipid-protein interactions
    • Rytömaa M., Kinnunen P.K.J. Reversibility of the binding of cytochrome c liposomes: implications for lipid-protein interactions. J. Biol. Chem. 1995, 270:3197-3202.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3197-3202
    • Rytömaa, M.1    Kinnunen, P.K.J.2
  • 14
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction: evidence for the extended lipid anchorage
    • Tuominen E.K., Wallace C.J., Kinnunen P.K.J. Phospholipid-cytochrome c interaction: evidence for the extended lipid anchorage. J. Biol. Chem. 2002, 277:8822-8826.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8822-8826
    • Tuominen, E.K.1    Wallace, C.J.2    Kinnunen, P.K.J.3
  • 15
    • 35048873629 scopus 로고    scopus 로고
    • Cytochrome c impaled: investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models
    • Kalanxhi E., Wallace C.J.A. Cytochrome c impaled: investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models. Biochem. J. 2007, 407:179-187.
    • (2007) Biochem. J. , vol.407 , pp. 179-187
    • Kalanxhi, E.1    Wallace, C.J.A.2
  • 19
    • 61749099621 scopus 로고    scopus 로고
    • Interaction of carbon monoxide with the apoptosis-inducing cytochrome c-cardiolipin complex
    • Kapetanaki S.M., Silkstone G., Husu I., Liebl U., Wilson M.T., Vos M.H. Interaction of carbon monoxide with the apoptosis-inducing cytochrome c-cardiolipin complex. Biochemistry 2009, 48:1613-1619.
    • (2009) Biochemistry , vol.48 , pp. 1613-1619
    • Kapetanaki, S.M.1    Silkstone, G.2    Husu, I.3    Liebl, U.4    Wilson, M.T.5    Vos, M.H.6
  • 20
    • 77953799127 scopus 로고    scopus 로고
    • Nitric oxide binds to the proximal heme coordination site of the ferrocytochrome c/cardiolipin complex: formation mechanism and dynamics
    • Silkstone G., Kapetanaki S.M., Husu I., Vos M.H., Wilson M.T. Nitric oxide binds to the proximal heme coordination site of the ferrocytochrome c/cardiolipin complex: formation mechanism and dynamics. J. Biol. Chem. 2010, 285:19785-19792.
    • (2010) J. Biol. Chem. , vol.285 , pp. 19785-19792
    • Silkstone, G.1    Kapetanaki, S.M.2    Husu, I.3    Vos, M.H.4    Wilson, M.T.5
  • 21
    • 0037119359 scopus 로고    scopus 로고
    • Protein oxidation of cytochrome c by reactive halogen species enhances its peroxidase activity
    • Chen Y.R., Deterding L.J., Sturgeon B.E., Tomer K.B., Mason R.P. Protein oxidation of cytochrome c by reactive halogen species enhances its peroxidase activity. J. Biol. Chem. 2002, 277:29781-29791.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29781-29791
    • Chen, Y.R.1    Deterding, L.J.2    Sturgeon, B.E.3    Tomer, K.B.4    Mason, R.P.5
  • 22
    • 0037195257 scopus 로고    scopus 로고
    • Peroxidase activity as a tool for studying the folding of c-type cytochromes
    • Diederix R.E., Ubbink M., Canters G.W. Peroxidase activity as a tool for studying the folding of c-type cytochromes. Biochemistry 2002, 41:13067-13077.
    • (2002) Biochemistry , vol.41 , pp. 13067-13077
    • Diederix, R.E.1    Ubbink, M.2    Canters, G.W.3
  • 28
    • 77955010738 scopus 로고    scopus 로고
    • Misfolded proteins and neurodegenerative diseases: mitochondrial dysfunction and role of nonnative states of cytochrome c in cell apoptosis
    • Santucci R., Sinibaldi F., Patriarca A., Santucci D., Fiorucci L. Misfolded proteins and neurodegenerative diseases: mitochondrial dysfunction and role of nonnative states of cytochrome c in cell apoptosis. Exp. Rev. Proteomics 2010, 7:507-517.
    • (2010) Exp. Rev. Proteomics , vol.7 , pp. 507-517
    • Santucci, R.1    Sinibaldi, F.2    Patriarca, A.3    Santucci, D.4    Fiorucci, L.5
  • 29
    • 58649095733 scopus 로고    scopus 로고
    • Nitration of solvent-exposed Tyrosine 74 on cytochrome c triggers heme iron-Methionine 80 bond disruption: nuclear magnetic resonance and optical spectroscopy studies
    • Abriata L.A., Cassina A., Tortora V., Marin M., Souza J.M., Castro L., Vila A.J., Radi R. Nitration of solvent-exposed Tyrosine 74 on cytochrome c triggers heme iron-Methionine 80 bond disruption: nuclear magnetic resonance and optical spectroscopy studies. J. Biol. Chem. 2009, 284:17-26.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17-26
    • Abriata, L.A.1    Cassina, A.2    Tortora, V.3    Marin, M.4    Souza, J.M.5    Castro, L.6    Vila, A.J.7    Radi, R.8
  • 30
    • 70449234614 scopus 로고
    • Spectrum of horse-heart cytochrome c
    • Margoliash E., Frohwirt N. Spectrum of horse-heart cytochrome c. Biochem. J. 1959, 71:570-572.
    • (1959) Biochem. J. , vol.71 , pp. 570-572
    • Margoliash, E.1    Frohwirt, N.2
  • 31
    • 0029688736 scopus 로고    scopus 로고
    • Syntheses of pure tetramethylammonium peroxynitrite
    • Bohle D.S., Glassbrenner P.A., Hansert B. Syntheses of pure tetramethylammonium peroxynitrite. Methods Enzymol. 1996, 269:302-311.
    • (1996) Methods Enzymol. , vol.269 , pp. 302-311
    • Bohle, D.S.1    Glassbrenner, P.A.2    Hansert, B.3
  • 32
    • 0029834589 scopus 로고    scopus 로고
    • Syntheses of peroxynitrite: to go with the flow or on solid grounds?
    • Koppenol W.H., Kissner R., Beckman J.S. Syntheses of peroxynitrite: to go with the flow or on solid grounds?. Methods Enzymol. 1996, 269:296-302.
    • (1996) Methods Enzymol. , vol.269 , pp. 296-302
    • Koppenol, W.H.1    Kissner, R.2    Beckman, J.S.3
  • 34
    • 0344844492 scopus 로고    scopus 로고
    • Metmyoglobin and methemoglobin catalyze the isomerization of peroxynitrite to nitrate
    • Herold S., Kalinga S. Metmyoglobin and methemoglobin catalyze the isomerization of peroxynitrite to nitrate. Biochemistry 2003, 42:14036-14046.
    • (2003) Biochemistry , vol.42 , pp. 14036-14046
    • Herold, S.1    Kalinga, S.2
  • 35
    • 3042771981 scopus 로고    scopus 로고
    • Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants
    • Herold S., Kalinga S., Matsui T., Watanabe Y. Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants. J. Am. Chem. Soc. 2004, 126:6945-6955.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6945-6955
    • Herold, S.1    Kalinga, S.2    Matsui, T.3    Watanabe, Y.4
  • 36
    • 21944443058 scopus 로고    scopus 로고
    • Chemistry of peroxynitrites and peroxynitrates
    • Goldstein S., Lind J., Merényi G. Chemistry of peroxynitrites and peroxynitrates. Chem. Rev. 2005, 105:2457-2470.
    • (2005) Chem. Rev. , vol.105 , pp. 2457-2470
    • Goldstein, S.1    Lind, J.2    Merényi, G.3
  • 37
    • 79951553268 scopus 로고    scopus 로고
    • Isoniazid and rifampicin inhibit allosterically heme binding to albumin and peroxynitrite isomerization by heme-albumin
    • Ascenzi P., Bolli A., di Masi A., Tundo G.R., Fanali G., Coletta M., Fasano M. Isoniazid and rifampicin inhibit allosterically heme binding to albumin and peroxynitrite isomerization by heme-albumin. J. Biol. Inorg. Chem. 2010, 10.1007/s00775-010-0706-2.
    • (2010) J. Biol. Inorg. Chem.
    • Ascenzi, P.1    Bolli, A.2    di Masi, A.3    Tundo, G.R.4    Fanali, G.5    Coletta, M.6    Fasano, M.7
  • 38
    • 78650892093 scopus 로고    scopus 로고
    • Drug binding to Sudlow's site I impairs allosterically human serum heme-albumin-catalyzed peroxynitrite detoxification
    • Ascenzi P., Bolli A., Gullotta F., Fanali G., Fasano M. Drug binding to Sudlow's site I impairs allosterically human serum heme-albumin-catalyzed peroxynitrite detoxification. IUBMB Life 2010, 62:776-780.
    • (2010) IUBMB Life , vol.62 , pp. 776-780
    • Ascenzi, P.1    Bolli, A.2    Gullotta, F.3    Fanali, G.4    Fasano, M.5
  • 39
    • 2542447171 scopus 로고    scopus 로고
    • Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress
    • Herold S., Fago A., Weber R.E., Dewilde S., Moens L. Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress. J. Biol. Chem. 2004, 279:22841-22847.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22841-22847
    • Herold, S.1    Fago, A.2    Weber, R.E.3    Dewilde, S.4    Moens, L.5


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