메뉴 건너뛰기




Volumn 1807, Issue 12, 2011, Pages 1616-1623

Nitration of tyrosines 46 and 48 induces the specific degradation of cytochrome c upon change of the heme iron state to high-spin

Author keywords

Apoptosis; High spin heme iron; Peroxidase activity; Post translational modification; Reactive nitrogen and oxygen species

Indexed keywords

CYTOCHROME C; HEME; PEROXIDASE; TYROSINE;

EID: 81155155485     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.09.012     Document Type: Article
Times cited : (35)

References (67)
  • 1
    • 33751112220 scopus 로고    scopus 로고
    • Oxidative stress in the pathogenesis of skin disease
    • DOI 10.1038/sj.jid.5700340, PII 5700340
    • D. Bickers, and M. Athar Oxidative stress in the pathogenesis of skin disease J. Invest. Dermatol. 126 2006 2565 2575 (Pubitemid 44764040)
    • (2006) Journal of Investigative Dermatology , vol.126 , Issue.12 , pp. 2565-2575
    • Bickers, D.R.1    Athar, M.2
  • 2
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: Central role of complex III
    • DOI 10.1074/jbc.M304854200
    • Q. Chen, E.J. Vazquez, S. Moghaddas, C.K. Hoppel, and E.J. Lesnefsky Production of reactive oxygen species by mitochondria: central role of complex III.J. Biol. Chem. 278 2003 36027 36031 (Pubitemid 37139922)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 3
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • DOI 10.1038/nrd2222, PII NRD2222
    • C. Szabó, H. Ischiropoulos, and R. Radi Peroxynitrite: biochemistry, pathophysiology and development of therapeutics Nat. Rev. Drug Discov. 6 2007 662 680 (Pubitemid 47207751)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.8 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 4
    • 58149350129 scopus 로고    scopus 로고
    • The proteasome and its role in the degradation of oxidized proteins
    • T. Jung, and T. Grune The proteasome and its role in the degradation of oxidized proteins IUBMB Life 60 2008 743 752
    • (2008) IUBMB Life , vol.60 , pp. 743-752
    • Jung, T.1    Grune, T.2
  • 6
    • 0036890524 scopus 로고    scopus 로고
    • Peroxynitrite reactions and formation in mitochondria
    • DOI 10.1016/S0891-5849(02)01111-5, PII S0891584902011115
    • R. Radi, A. Cassina, R. Hodara, C. Quijano, and L. Castro Peroxynitrite reactions and formation in mitochondria Free Radic. Biol. Med. 33 2002 1451 1464 (Pubitemid 35351588)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.11 , pp. 1451-1464
    • Radi, R.1    Cassina, A.2    Hodara, R.3    Quijano, C.4    Castro, L.5
  • 7
    • 0029037495 scopus 로고
    • The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
    • W.A. Pryor, and G.L. Squadrito The chemistry of peroxynitrite: a product from the reaction of nitric oxide with superoxide Am. J. Physiol. Lung Cell. Mol. Physiol. 268 1995 L699 L722
    • (1995) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.268
    • Pryor, W.A.1    Squadrito, G.L.2
  • 9
    • 34249827861 scopus 로고    scopus 로고
    • Oxidized proteins: Intracellular distribution and recognition by the proteasome
    • DOI 10.1016/j.abb.2007.01.030, PII S0003986107000367, Highlight Issue: Pro- and antiapoptotic Signalling
    • T. Jung, N. Bader, and T. Grune Oxidized proteins: intracellular distribution and recognition by the proteasome Arch. Biochem. Biophys. 462 2007 231 237 (Pubitemid 46856318)
    • (2007) Archives of Biochemistry and Biophysics , vol.462 , Issue.2 , pp. 231-237
    • Jung, T.1    Bader, N.2    Grune, T.3
  • 10
    • 77955460506 scopus 로고    scopus 로고
    • Mechanisms of peroxynitrite interactions with heme proteins
    • J. Su, and J.T. Groves Mechanisms of peroxynitrite interactions with heme proteins Inorg. Chem. 49 2010 6317 6329
    • (2010) Inorg. Chem. , vol.49 , pp. 6317-6329
    • Su, J.1    Groves, J.T.2
  • 12
    • 0029133296 scopus 로고
    • Quantitation of protein tyrosine, 3-nitrotyrosine, and 3-aminotyrosine utilizing HPLC and intrinsic ultraviolet absorbance
    • J.P. Crow, and J.S. Beckman Quantitation of protein tyrosine, 3-nitrotyrosine, and 3-aminotyrosine utilizing HPLC and intrinsic ultraviolet absorbance Methods 7 1995 116 120
    • (1995) Methods , vol.7 , pp. 116-120
    • Crow, J.P.1    Beckman, J.S.2
  • 13
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: A pathophysiological function of nitric oxide and reactive oxygen species
    • DOI 10.1006/abbi.1998.0755
    • H. Ischiropoulos Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species Arch. Biochem. Biophys. 356 1998 1 11 (Pubitemid 28364347)
    • (1998) Archives of Biochemistry and Biophysics , vol.356 , Issue.1 , pp. 1-11
    • Ischiropoulos, H.1
  • 14
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: Localisation, quantification, consequences for protein function and signal transduction
    • S.A. Greenacre, and H. Ischiropoulos Tyrosine nitration: localization, quantification, consequences for protein function and signal transduction Free Radic. Res. 34 2001 541 581 (Pubitemid 32694646)
    • (2001) Free Radical Research , vol.34 , Issue.6 , pp. 541-581
    • Greenacre, S.1    Ischiropoulos, H.2
  • 18
    • 0033150608 scopus 로고    scopus 로고
    • Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite
    • DOI 10.1006/abbi.1999.1202
    • L.A. MacMillan-Crow, and J.A. Thompson Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite Arch. Biochem. Biophys. 366 1999 82 88 (Pubitemid 29394232)
    • (1999) Archives of Biochemistry and Biophysics , vol.366 , Issue.1 , pp. 82-88
    • MacMillan-Crow, L.A.1    Thompson, J.A.2
  • 23
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • DOI 10.1016/S0092-8674(00)80085-9
    • X. Liu, C.N. Kim, J. Yang, R. Jemmerson, and X. Wang Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c Cell 86 1996 147 157 (Pubitemid 26256586)
    • (1996) Cell , vol.86 , Issue.1 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 24
    • 0032504574 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: The role of cytochrome c
    • DOI 10.1016/S0005-2728(98)00109-1, PII S0005272898001091
    • J. Cai, J. Yang, and D.P. Jones Mitochondrial control of apoptosis: the role of cytochrome c Biochim. Biophys. Acta 1366 1998 139 149 (Pubitemid 28467028)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1366 , Issue.1-2 , pp. 139-149
    • Cai, J.1    Yang, J.2    Jones, D.P.3
  • 25
    • 20144370272 scopus 로고    scopus 로고
    • Time course and site(s) of cytochrome c tyrosine nitration by peroxynitrite
    • DOI 10.1021/bi0474620
    • C. Batthyány, J.M. Souza, R. Durán, A. Cassina, C. Cerveñansky, and R. Radi Time course and site(s) of cytochrome c tyrosine nitration by peroxynitrite Biochemistry 44 2005 8038 8046 (Pubitemid 40776665)
    • (2005) Biochemistry , vol.44 , Issue.22 , pp. 8038-8046
    • Batthyany, C.1    Souza, J.M.2    Duran, R.3    Cassina, A.4    Cervenansky, C.5    Radi, R.6
  • 26
    • 56749136365 scopus 로고    scopus 로고
    • Effect of nitration on the physicochemical and kinetic features of wild-type and monotyrosine mutants of human respiratory cytochrome c
    • V. Rodríguez-Roldán, J.M. García-Heredia, J.A. Navarro, M.A. De la Rosa, and M. Hervás Effect of nitration on the physicochemical and kinetic features of wild-type and monotyrosine mutants of human respiratory cytochrome c Biochemistry 47 2008 12371 12379
    • (2008) Biochemistry , vol.47 , pp. 12371-12379
    • Rodríguez-Roldán, V.1    García-Heredia, J.M.2    Navarro, J.A.3    De La Rosa, M.A.4    Hervás, M.5
  • 27
    • 0037352488 scopus 로고    scopus 로고
    • Tyrosine-nitration of caspase 3 and cytochrome C does not suppress apoptosis induction in squamous cell carcinoma cells
    • DOI 10.1002/ijc.10832
    • E. Ueta, T. Kamatani, T. Yamamoto, and T. Osaki Tyrosine-nitration of caspase 3 and cytochrome c does not suppress apoptosis induction in squamous cell carcinoma cells Int. J. Cancer 103 2003 717 722 (Pubitemid 36110226)
    • (2003) International Journal of Cancer , vol.103 , Issue.6 , pp. 717-722
    • Ueta, E.1    Kamatani, T.2    Yamamoto, T.3    Osaki, T.4
  • 31
    • 27944453616 scopus 로고    scopus 로고
    • Biochemical properties of cytochrome c nitrated by peroxynitrite
    • B. Jang, and S. Han Biochemical properties of cytochrome c nitrated by peroxynitrite Biochimie 88 2005 53 58
    • (2005) Biochimie , vol.88 , pp. 53-58
    • Jang, B.1    Han, S.2
  • 34
    • 7544224011 scopus 로고    scopus 로고
    • Interaction of calmodulin with the phosphofructokinase target sequence
    • DOI 10.1016/j.febslet.2004.10.023, PII S0014579304012578
    • S.R. Martin, R.R. Biekofsky, M.A. Skinner, R. Guerrini, S. Salvadori, J. Feeney, and P.M. Bayley Interaction of calmodulin with the phosphofructokinase target sequence FEBS Lett. 577 2004 284 288 (Pubitemid 39452399)
    • (2004) FEBS Letters , vol.577 , Issue.1-2 , pp. 284-288
    • Martin, S.R.1    Biekofsky, R.R.2    Skinner, M.A.3    Guerrini, R.4    Salvadori, S.5    Feeney, J.6    Bayley, P.M.7
  • 35
    • 0000370821 scopus 로고
    • Solvent peak saturation with single phase and quadrature Fourier transformation
    • D.I. Hoult Solvent peak saturation with single phase and quadrature Fourier transformation J. Magn. Reson. 21 1976 337 347
    • (1976) J. Magn. Reson. , vol.21 , pp. 337-347
    • Hoult, D.I.1
  • 36
    • 49049126489 scopus 로고
    • Efficient detection of paramagnetically shifted NMR resonances by optimizing the WEFT pulse sequence
    • I. Inubushi, and E.D. Becker Efficient detection of paramagnetically shifted NMR resonances by optimizing the WEFT pulse sequence J. Magn. Reson. 51 1983 128 133
    • (1983) J. Magn. Reson. , vol.51 , pp. 128-133
    • Inubushi, I.1    Becker, E.D.2
  • 37
    • 0004039284 scopus 로고
    • P.D. Boyer, Academic Press New York
    • R.E. Dickerson, and R. Timkovich The Enzymes P.D. Boyer, 1995 Academic Press New York 397 547
    • (1995) The Enzymes , pp. 397-547
    • Dickerson, R.E.1    Timkovich, R.2
  • 39
    • 0015967881 scopus 로고
    • Conformational, parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins
    • P.Y. Chou, and G.D. Fasman Conformational, parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins Biochemistry 13 1974 211 272
    • (1974) Biochemistry , vol.13 , pp. 211-272
    • Chou, P.Y.1    Fasman, G.D.2
  • 40
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • DOI 10.1152/physrev.00029.2006
    • P. Pacher, J. Beckman, and L. Liaudet Nitric oxide and peroxynitrite in health and disease Physiol. Rev. 87 2007 315 424 (Pubitemid 46217686)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 41
    • 49049126489 scopus 로고
    • Efficient detection of paramagnetically shifted NMR resonances by optimizing the WEFT pulse sequence
    • I. Inubushi, and E.D. Becker Efficient detection of paramagnetically shifted NMR resonances by optimizing the WEFT pulse sequence J. Magn. Reson. 51 1983 128 133
    • (1983) J. Magn. Reson. , vol.51 , pp. 128-133
    • Inubushi, I.1    Becker, E.D.2
  • 42
    • 0017171066 scopus 로고
    • [Nitrotyrosyl]cytochrome c: Studies of the effect of iron binding, protein denaturants and oxidation-reduction potentials
    • A.G. Do Nascimento [Nitrotyrosyl]cytochrome c: studies of the effect of iron binding, protein denaturants and oxidation-reduction potentials Biochem. J. 155 1976 589 597
    • (1976) Biochem. J. , vol.155 , pp. 589-597
    • Do Nascimento, A.G.1
  • 43
    • 0040454530 scopus 로고
    • PH and temperature effect on the absorption spectra of Pseudomonas aeruginosa cytochrome c-551 solution
    • Y. Li, K. Imaeda, and H. Inokuchi pH and temperature effect on the absorption spectra of Pseudomonas aeruginosa cytochrome c-551 solution J. Phys. Chem. 98 1994 4726 4728
    • (1994) J. Phys. Chem. , vol.98 , pp. 4726-4728
    • Li, Y.1    Imaeda, K.2    Inokuchi, H.3
  • 44
    • 0027199762 scopus 로고
    • Optical activity of hemoproteins in the Soret region. Circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution
    • G. Blauer, N. Sreerama, and R.M. Woody Optical activity of hemoproteins in the soret region. Circular dichroism of the heme undecapeptide of cytochrome Biochemistry 32 1993 6674 6679 (Pubitemid 23217137)
    • (1993) Biochemistry , vol.32 , Issue.26 , pp. 6674-6679
    • Blauer, G.1    Sreerama, N.2    Woody, R.W.3
  • 45
    • 0030727547 scopus 로고    scopus 로고
    • The soret circular dichroism spectrum as a probe for the heme Fe(III)- Met(80) axial bond in horse cytochrome c
    • DOI 10.1016/S0162-0134(97)00100-1, PII S0162013497001001
    • R. Santucci, and F. Ascoli The Soret circular dichroism spectrum as a probe for the heine Fe(III)-Met(80) axial bond in horse cytochrome c J. Inorg. Biochem. 68 1997 211 214 (Pubitemid 27459390)
    • (1997) Journal of Inorganic Biochemistry , vol.68 , Issue.3 , pp. 211-214
    • Santucci, R.1    Ascoli, F.2
  • 46
    • 0020478683 scopus 로고
    • Spin state and unfolding equilibria of ferricytochrome c in acidic solutions
    • H.J. Dyson, and J.K. Beattie Spin state and unfolding equilibria of ferricytochrome c in acidic solutions J. Biol. Chem. 257 1982 2267 2273
    • (1982) J. Biol. Chem. , vol.257 , pp. 2267-2273
    • Dyson, H.J.1    Beattie, J.K.2
  • 48
    • 0032508940 scopus 로고    scopus 로고
    • Alkaline conformational transitions of ferricytochrome c studied by resonance Raman spectroscopy
    • DOI 10.1021/ja9717572
    • S. Döpner, P. Hildebrandt, F.I. Rossell, and A.G. Mauk Alkaline conformational transitions of ferricytochrome c studied by resonance raman spectroscopy J. Am. Chem. Soc. 120 1998 11246 11255 (Pubitemid 28531065)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.44 , pp. 11246-11255
    • Dopner, S.1    Hildebrandt, P.2    Resell, F.I.3    Mauk, A.G.4
  • 49
    • 0024596945 scopus 로고
    • NMR study of the alkaline isomerization of ferricytochrome c
    • DOI 10.1016/0014-5793(89)80262-5
    • X.L. Hong, and D.W. Dixon NMR study of the alkaline isomerization of ferricytochrome c FEBS Lett. 246 1989 105 108 (Pubitemid 19087780)
    • (1989) FEBS Letters , vol.246 , Issue.1-2 , pp. 105-108
    • Hong, X.1    Dixon, D.W.2
  • 52
    • 84655163936 scopus 로고    scopus 로고
    • Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch
    • doi:10.1007/s00775-011-0804-9 (in press), doi
    • J.M. García-Heredia, A. Díaz-Quintana, M. Salzano, M. Orzáez, E. Pérez-Payá, M. Teixeira, M.A. De la Rosa, I. Díaz-Moreno, Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch, J. Biol. Inorg. Chem. (in press), doi: 10.1007/s00775-011-0804-9.
    • J. Biol. Inorg. Chem.
    • García-Heredia, J.M.1
  • 53
    • 0016256727 scopus 로고
    • Alkaline isomerization of oxidized cytochrome c
    • L. Davids, A. Schejter, and G. Hess Alkaline isomerization of oxidized cytochrome c J. Biol. Chem. 249 1974 2624 2632
    • (1974) J. Biol. Chem. , vol.249 , pp. 2624-2632
    • Davids, L.1    Schejter, A.2    Hess, G.3
  • 55
    • 10644249922 scopus 로고    scopus 로고
    • Native, not nitrated, cytochrome c and mitochondria-derived peroxide drive osteoclast apoptosis
    • M.J. Oursler, E.W. Bradley, S.L. Elfering, and C. Giulivi Native, not nitrated, cytochrome c and mitochondria-derived peroxide drive osteoclast apoptosis Am. J. Physiol. Cell Physiol. 288 2005 C156 C168
    • (2005) Am. J. Physiol. Cell Physiol. , vol.288
    • Oursler, M.J.1    Bradley, E.W.2    Elfering, S.L.3    Giulivi, C.4
  • 57
    • 33845379583 scopus 로고
    • Control of heme protein redox potential and reduction rate: Linear free energy relation between potential and ferric spin state equilibrium
    • M.T. Fisher, and S.G. Sligar Control of heme protein redox potential and reduction rate: linear free energy relation between potential and ferric spin state equilibrium J. Am. Chem. Soc. 107 1985 5018 5019
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5018-5019
    • Fisher, M.T.1    Sligar, S.G.2
  • 60
    • 77955235585 scopus 로고    scopus 로고
    • Phosphomimetic substitution of cytochrome c tyrosine 48 decreases respiration and binding to cardiolipin and abolishes ability to trigger downstream caspase activation
    • P. Pecina, G.G. Borisenko, N.A. Belikova, Y. Tyurina, A. Pecinova, I. Lee, A.K. Samhan-Arias, K. Przyklenk, V.E. Kagan, and M. Huttemann Phosphomimetic substitution of cytochrome c tyrosine 48 decreases respiration and binding to cardiolipin and abolishes ability to trigger downstream caspase activation Biochemistry 49 2010 6705 6714
    • (2010) Biochemistry , vol.49 , pp. 6705-6714
    • Pecina, P.1    Borisenko, G.G.2    Belikova, N.A.3    Tyurina, Y.4    Pecinova, A.5    Lee, I.6    Samhan-Arias, A.K.7    Przyklenk, K.8    Kagan, V.E.9    Huttemann, M.10
  • 61
    • 35048873629 scopus 로고    scopus 로고
    • Cytochrome c impaled: Investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models
    • DOI 10.1042/BJ20070459
    • E. Kalanxhi, and C.J.A. Wallace Cytochrome c impaled: investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models Biochem. J. 407 2007 179 187 (Pubitemid 47556983)
    • (2007) Biochemical Journal , vol.407 , Issue.2 , pp. 179-187
    • Kalanxhi, E.1    Wallace, C.J.A.2
  • 65
    • 46349095835 scopus 로고    scopus 로고
    • Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo, inhibiting mitochondrial respiration
    • H. Yu, I. Lee, A.R. Salomon, K. Yu, and M. Hüttemann Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo, inhibiting mitochondrial respiration Biochim. Biophys. Acta 1777 2008 1066 1071
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1066-1071
    • Yu, H.1    Lee, I.2    Salomon, A.R.3    Yu, K.4    Hüttemann, M.5
  • 66
    • 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
    • M. Hüttemann, P. Pecina, M. Rainbolt, T.H. Sanderson, V.E. Kagan, L. Samavati, J.W. Doan, and I. Lee The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: from respiration to apoptosis Mitochondrion 11 2011 369 381
    • (2011) Mitochondrion , vol.11 , pp. 369-381
    • Hüttemann, 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
  • 67
    • 0029983162 scopus 로고    scopus 로고
    • Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: Lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH2 peptide
    • S.K. Kong, M.B. Yim, E.R. Stadtman, and P.B. Chock Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH2 peptide Proc. Natl. Acad. Sci. U.S.A. 93 1996 3377 33782
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 3377-33782
    • Kong, S.K.1    Yim, M.B.2    Stadtman, E.R.3    Chock, P.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.