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Volumn 415, Issue 3, 2011, Pages 463-467

Peroxynitrite detoxification by horse heart carboxymethylated cytochrome c is allosterically modulated by cardiolipin

Author keywords

Allostery; Carboxymethylated cytochrome c; Cardiolipin bound carboxymethylated cytochrome c; Horse heart cytochrome c; Kinetics; Peroxynitrite isomerization

Indexed keywords

CARBOXYMETHYLATED CYTOCHROME C; CARDIOLIPIN; CYTOCHROME C; FERRIC ION; HEME; PEROXYNITRITE; UNCLASSIFIED DRUG;

EID: 82355190054     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.10.094     Document Type: Article
Times cited : (23)

References (56)
  • 3
    • 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
  • 4
    • 0019888571 scopus 로고
    • Conformation change of cytochrome c: II - ferricytochrome c refinement at 1.8å comparison with the ferrocytochrome structure
    • Takano T., Dickerson R.E. Conformation change of cytochrome c: II - ferricytochrome c refinement at 1.8å comparison with the ferrocytochrome structure. J. Mol. Biol. 1981, 153:95-115.
    • (1981) J. Mol. Biol. , vol.153 , pp. 95-115
    • Takano, T.1    Dickerson, R.E.2
  • 5
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell G.W., Louie G.V., Brayer G.D. High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 1990, 214:585-595.
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 7
    • 0014216555 scopus 로고
    • The reactivity of ferricytochrome c with ionic ligands
    • George P., Glauser S.C., Schejter A. The reactivity of ferricytochrome c with ionic ligands. J. Biol. Chem. 1967, 242:1690-1695.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1690-1695
    • George, P.1    Glauser, S.C.2    Schejter, A.3
  • 8
    • 0015502050 scopus 로고
    • Mechanisms of the reactions of cytochrome c: rate and equilibrium constants for ligand binding to horse heart ferricytochrome c
    • Sutin N., Yandell J.K. Mechanisms of the reactions of cytochrome c: rate and equilibrium constants for ligand binding to horse heart ferricytochrome c. J. Biol. Chem. 1972, 247:6932-6936.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6932-6936
    • Sutin, N.1    Yandell, J.K.2
  • 9
    • 0017414776 scopus 로고
    • 15 N-resonances in cyanide complexes of myoglobin and cytochrome c and some implications for their heme environmental structures
    • 15 N-resonances in cyanide complexes of myoglobin and cytochrome c and some implications for their heme environmental structures. FEBS Lett. 1977, 81:57-60.
    • (1977) FEBS Lett. , vol.81 , pp. 57-60
    • Morishima, I.1    Inubushi, T.2
  • 10
    • 0002014257 scopus 로고
    • Ligand binding to cytochrome c and other related haem proteins and peptides: part I - equilibrium studies
    • Saleem M.M.M., Wilson M.T. Ligand binding to cytochrome c and other related haem proteins and peptides: part I - equilibrium studies. Inorg. Chim. Acta 1988, 153:93-98.
    • (1988) Inorg. Chim. Acta , vol.153 , pp. 93-98
    • Saleem, M.M.M.1    Wilson, M.T.2
  • 11
    • 0002014259 scopus 로고
    • Ligand binding to cytochrome c and other related haem proteins and peptides: part II - kinetic studies
    • Saleem M.M.M., Wilson M.T. Ligand binding to cytochrome c and other related haem proteins and peptides: part II - kinetic studies. Inorg. Chim. Acta 1988, 153:99-104.
    • (1988) Inorg. Chim. Acta , vol.153 , pp. 99-104
    • Saleem, M.M.M.1    Wilson, M.T.2
  • 12
    • 0028340452 scopus 로고
    • Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative: a spectroscopic and thermodynamic study
    • Ascenzi P., Coletta M., Santucci R., Polizio F., Desideri A. Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative: a spectroscopic and thermodynamic study. J. Inorg. Biochem. 1994, 53:273-280.
    • (1994) J. Inorg. Biochem. , vol.53 , pp. 273-280
    • Ascenzi, P.1    Coletta, M.2    Santucci, R.3    Polizio, F.4    Desideri, A.5
  • 13
    • 0029867909 scopus 로고    scopus 로고
    • Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative: a comparative study
    • Viola F., Aime S., Coletta M., Desideri A., Fasano M., Paoletti S., Tarricone C., Ascenzi P. Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative: a comparative study. J. Inorg. Biochem. 1996, 62:213-222.
    • (1996) J. Inorg. Biochem. , vol.62 , pp. 213-222
    • Viola, F.1    Aime, S.2    Coletta, M.3    Desideri, A.4    Fasano, M.5    Paoletti, S.6    Tarricone, C.7    Ascenzi, P.8
  • 14
    • 0030036756 scopus 로고    scopus 로고
    • Studies on the reaction mechanism for reductive nitrosylation of ferrihemoproteins in buffer solutions
    • Hoshino M., Maeda M., Konishi R., Seki H., Ford P.C. Studies on the reaction mechanism for reductive nitrosylation of ferrihemoproteins in buffer solutions. J. Am. Chem. Soc. 1996, 118:5702-5707.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5702-5707
    • Hoshino, M.1    Maeda, M.2    Konishi, R.3    Seki, H.4    Ford, P.C.5
  • 16
    • 0038381423 scopus 로고    scopus 로고
    • Nitrosylation of cytochrome c during apoptosis
    • Schonhoff C.M., Gaston B., Mannick J.B. Nitrosylation of cytochrome c during apoptosis. J. Biol. Chem. 2003, 278:18265-18270.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18265-18270
    • Schonhoff, C.M.1    Gaston, B.2    Mannick, J.B.3
  • 17
    • 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
  • 19
    • 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
  • 20
    • 0014314436 scopus 로고
    • Carboxymethylation of horse heart ferricytochrome c and cyanferricytochrome c
    • Stellwagen E. Carboxymethylation of horse heart ferricytochrome c and cyanferricytochrome c. Biochemistry 1968, 7:2496-2501.
    • (1968) Biochemistry , vol.7 , pp. 2496-2501
    • Stellwagen, E.1
  • 21
    • 0023645247 scopus 로고
    • Unfolding and flexibility in hemoproteins shown in the case of carboxymethylated cytochrome c
    • Santucci R., Brunori M., Ascoli F. Unfolding and flexibility in hemoproteins shown in the case of carboxymethylated cytochrome c. Biochim. Biophys. Acta 1987, 914:185-189.
    • (1987) Biochim. Biophys. Acta , vol.914 , pp. 185-189
    • Santucci, R.1    Brunori, M.2    Ascoli, F.3
  • 22
    • 0024821289 scopus 로고
    • Structural transitions of carboxymethylated cytochrome c: calorimetric and circular dichroism studies
    • Santucci R., Giartosio A., Ascoli F. Structural transitions of carboxymethylated cytochrome c: calorimetric and circular dichroism studies. Arch. Biochem. Biophys. 1989, 275:496-504.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 496-504
    • Santucci, R.1    Giartosio, A.2    Ascoli, F.3
  • 23
    • 0036538798 scopus 로고    scopus 로고
    • Reaction of hydrogen peroxide and peroxidase activity in carboxymethylated cytochrome c: spectroscopic and kinetic studies
    • Prasad S., Maiti N.C., Mazumdar S., Mitra S. Reaction of hydrogen peroxide and peroxidase activity in carboxymethylated cytochrome c: spectroscopic and kinetic studies. Biochim. Biophys. Acta 2002, 1596:63-75.
    • (2002) Biochim. Biophys. Acta , vol.1596 , pp. 63-75
    • Prasad, S.1    Maiti, N.C.2    Mazumdar, S.3    Mitra, S.4
  • 24
    • 0013846674 scopus 로고
    • Production of a " cytochrome c " with myoglobin-like properties by alkylating the cyanide complex with bromoacetate
    • Schejter A., George P. Production of a " cytochrome c " with myoglobin-like properties by alkylating the cyanide complex with bromoacetate. Nature 1965, 206:1150-1151.
    • (1965) Nature , vol.206 , pp. 1150-1151
    • Schejter, A.1    George, P.2
  • 25
    • 0014939335 scopus 로고
    • The effects of alkylation of methionyl residues on the properties of horse cytochrome c
    • Schejter A., Aviram I. The effects of alkylation of methionyl residues on the properties of horse cytochrome c. J. Biol. Chem. 1970, 245:1552-1557.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1552-1557
    • Schejter, A.1    Aviram, I.2
  • 26
    • 0015718124 scopus 로고
    • Properties of modified cytochromes: II - ligand binding to reduced carboxymethyl cytochrome c
    • Wilson M.T., Brunori M., Rotilio G.C., Antonini E. Properties of modified cytochromes: II - ligand binding to reduced carboxymethyl cytochrome c. J. Biol. Chem. 1973, 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
  • 27
    • 0016221760 scopus 로고
    • The structure of the heme crevice of ferric cytochrome c alkylated at methionine-80
    • Aviram I., Krauss Y. The structure of the heme crevice of ferric cytochrome c alkylated at methionine-80. J. Biol. Chem. 1974, 249:2575-2578.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2575-2578
    • Aviram, I.1    Krauss, Y.2
  • 28
    • 0023677342 scopus 로고
    • The binding characteristics of the cytochrome c iron
    • Schejter A., Plotkin B. The binding characteristics of the cytochrome c iron. Biochem. J. 1988, 255:353-356.
    • (1988) Biochem. J. , vol.255 , pp. 353-356
    • Schejter, A.1    Plotkin, B.2
  • 30
    • 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
  • 31
    • 79953239495 scopus 로고    scopus 로고
    • Cardiolipin drives cytochrome c proapoptotic and antiapoptotic actions
    • Ascenzi P., Polticelli F., Marino M., Santucci R., Coletta M. Cardiolipin drives cytochrome c proapoptotic and antiapoptotic actions. IUBMB Life 2011, 63:160-165.
    • (2011) IUBMB Life , vol.63 , pp. 160-165
    • Ascenzi, P.1    Polticelli, F.2    Marino, M.3    Santucci, R.4    Coletta, M.5
  • 32
    • 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
  • 33
    • 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
  • 34
    • 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
  • 38
    • 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
  • 39
    • 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
  • 40
    • 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
  • 45
    • 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
  • 47
    • 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
  • 48
    • 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
  • 49
    • 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
  • 50
    • 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
  • 51
    • 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. 2011, 16:97-108.
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 97-108
    • Ascenzi, P.1    Bolli, A.2    di Masi, A.3    Tundo, G.R.4    Fanali, G.5    Coletta, M.6    Fasano, M.7
  • 52
    • 0014006570 scopus 로고
    • Alkylation of cytochromes c: I - properties of alkylated beef cytochrome c
    • Ando K., Matsubara H., Okonuki K. Alkylation of cytochromes c: I - properties of alkylated beef cytochrome c. Biochim. Biophys. Acta 1966, 118:240-255.
    • (1966) Biochim. Biophys. Acta , vol.118 , pp. 240-255
    • Ando, K.1    Matsubara, H.2    Okonuki, K.3
  • 55
    • 0017364802 scopus 로고
    • The reduction by dithionite of Fe(III) myoglobin derivatives with different ligands attached to the iron atom: a study by rapid-wavelength-scanning stopped-flow spectrophotometry
    • Cox R.P., Hollaway M.R. The reduction by dithionite of Fe(III) myoglobin derivatives with different ligands attached to the iron atom: a study by rapid-wavelength-scanning stopped-flow spectrophotometry. Eur. J. Biochem. 1977, 74:575-587.
    • (1977) Eur. J. Biochem. , vol.74 , pp. 575-587
    • Cox, R.P.1    Hollaway, M.R.2
  • 56
    • 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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