메뉴 건너뛰기




Volumn 38, Issue 2, 2005, Pages 201-214

Mechanism of hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation as explored by immuno-spin trapping: The role of copper- and carbonate radical anion-mediated oxidations

Author keywords

5,5 Dimethyl 1 pyrroline N Oxide; Carbonate radical anion; Copper catalyzed oxidation; Cu,Zn superoxide dismutase radical derived nitrone adduct; Dityrosine; Hydrogen peroxide; Immuno spin trapping; Superoxide dismutase

Indexed keywords

CARBONIC ACID; COPPER; CYANIDE; HYDROGEN PEROXIDE; RADICAL; SUPEROXIDE DISMUTASE; ZINC;

EID: 10644225292     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.10.008     Document Type: Article
Times cited : (55)

References (55)
  • 1
  • 3
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymic function for erythrocuprein (hemocuprein)
    • J.M. McCord, and I. Fridovich Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein) J. Biol. Chem. 244 1969 6049 6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 4
    • 0033555968 scopus 로고    scopus 로고
    • Bicarbonate is required for the peroxidase function of Cu, Zn-superoxide dismutase at physiological pH
    • S. Sankarapandi, and J.L. Zweier Bicarbonate is required for the peroxidase function of Cu, Zn-superoxide dismutase at physiological pH J. Biol. Chem. 274 1999 1226 1232
    • (1999) J. Biol. Chem. , vol.274 , pp. 1226-1232
    • Sankarapandi, S.1    Zweier, J.L.2
  • 5
    • 0027456505 scopus 로고
    • Enzyme function of copper, zinc superoxide dismutase as a free radical generator
    • M.B. Yim, P.B. Chock, and E.R. Stadtman Enzyme function of copper, zinc superoxide dismutase as a free radical generator J. Biol. Chem. 268 1993 4099 4105
    • (1993) J. Biol. Chem. , vol.268 , pp. 4099-4105
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 8
    • 0029846920 scopus 로고    scopus 로고
    • Peroxynitrite-dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase, and horseradish peroxidase
    • J.B. Sampson, H. Rosen, and J.S. Beckman Peroxynitrite-dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase, and horseradish peroxidase Methods Enzymol. 269 1996 210 218
    • (1996) Methods Enzymol. , vol.269 , pp. 210-218
    • Sampson, J.B.1    Rosen, H.2    Beckman, J.S.3
  • 9
    • 0037127295 scopus 로고    scopus 로고
    • Thiol oxidase activity of copper, zinc superoxide dismutase
    • C.C. Winterbourn, A.V. Peskin, and H.N. Parsons-Mair Thiol oxidase activity of copper, zinc superoxide dismutase J. Biol. Chem. 277 2002 1906 1911
    • (2002) J. Biol. Chem. , vol.277 , pp. 1906-1911
    • Winterbourn, C.C.1    Peskin, A.V.2    Parsons-Mair, H.N.3
  • 10
    • 0016816805 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Chemiluminescence and peroxidation
    • E.K. Hodgson, and I. Fridovich The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation Biochemistry 14 1975 5299 5303
    • (1975) Biochemistry , vol.14 , pp. 5299-5303
    • Hodgson, E.K.1    Fridovich, I.2
  • 11
    • 0033405524 scopus 로고    scopus 로고
    • On the role of bicarbonate in peroxidations catalyzed by Cu,Zn superoxide dismutase
    • S.I. Liochev, and I. Fridovich On the role of bicarbonate in peroxidations catalyzed by Cu,Zn superoxide dismutase Free Radic. Biol. Med. 27 1999 1444 1447
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 1444-1447
    • Liochev, S.I.1    Fridovich, I.2
  • 12
    • 0347337781 scopus 로고    scopus 로고
    • Bicarbonate-enhanced peroxidase activity of Cu,ZnSOD: Is the distal oxidant bound or diffusible?
    • S.I. Liochev, and I. Fridovich Bicarbonate-enhanced peroxidase activity of Cu,ZnSOD: is the distal oxidant bound or diffusible? Arch. Biochem. Biophys. 421 2004 255 259
    • (2004) Arch. Biochem. Biophys. , vol.421 , pp. 255-259
    • Liochev, S.I.1    Fridovich, I.2
  • 13
    • 0027980816 scopus 로고
    • 2: Selective generation of 2-oxo-histidine at the histidine 118
    • 2: selective generation of 2-oxo-histidine at the histidine 118 J. Biol. Chem. 269 1994 2405 2410
    • (1994) J. Biol. Chem. , vol.269 , pp. 2405-2410
    • Uchida, K.1    Kawakishi, S.2
  • 14
    • 0035955156 scopus 로고    scopus 로고
    • 2-treated Cu,Zn-SOD protein with LC-ESI-Q-TOF-MS, MS/MS for the determination of the copper-binding site
    • 2-treated Cu,Zn-SOD protein with LC-ESI-Q-TOF-MS, MS/MS for the determination of the copper-binding site J. Am. Chem. Soc. 123 2001 9268 9278
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9268-9278
    • Kurahashi, T.1    Miyazaki, A.2    Suwan, S.3    Isobe, M.4
  • 15
    • 0026469348 scopus 로고
    • 2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme
    • 2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme J. Biol. Chem. 267 1992 25371 25377
    • (1992) J. Biol. Chem. , vol.267 , pp. 25371-25377
    • Sato, K.1    Akaike, T.2    Kohno, M.3    Ando, M.4    Maeda, H.5
  • 17
    • 0020570983 scopus 로고
    • Copper salt-dependent hydroxyl radical formation. Damage to proteins acting as antioxidants
    • J.M.C. Gutteridge, and S. Wilkins Copper salt-dependent hydroxyl radical formation. Damage to proteins acting as antioxidants Biochim. Biophys. Acta 759 1983 38 41
    • (1983) Biochim. Biophys. Acta , vol.759 , pp. 38-41
    • Gutteridge, J.M.C.1    Wilkins, S.2
  • 18
    • 0023732274 scopus 로고
    • A site-specific mechanism for free radical induced biological damage: The essential role of redox-active transition metals
    • M. Chevion A site-specific mechanism for free radical induced biological damage: the essential role of redox-active transition metals Free Radic. Biol. Med. 5 1988 27 37
    • (1988) Free Radic. Biol. Med. , vol.5 , pp. 27-37
    • Chevion, M.1
  • 19
    • 0031023945 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated degradation of protein: Different oxidation modes of copper- and iron-dependent hydroxyl radicals on the degradation of albumin
    • T. Kocha, M. Yamaguchi, H. Ohtaki, T. Fukuda, and T. Aoyagi Hydrogen peroxide-mediated degradation of protein: different oxidation modes of copper- and iron-dependent hydroxyl radicals on the degradation of albumin Biochim. Biophys. Acta 1337 1997 319 326
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 319-326
    • Kocha, T.1    Yamaguchi, M.2    Ohtaki, H.3    Fukuda, T.4    Aoyagi, T.5
  • 20
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • C.L. Hawkins, and M.J. Davies Generation and propagation of radical reactions on proteins Biochim. Biophys. Acta 1504 2001 196 219
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 21
    • 0034640515 scopus 로고    scopus 로고
    • Bicarbonate enhances the hydroxylation, nitration, and peroxidation reactions catalyzed by copper, zinc superoxide dismutase: Intermediacy of carbonate anion radical
    • H. Zhang, J. Joseph, C. Felix, and B. Kalyanaraman Bicarbonate enhances the hydroxylation, nitration, and peroxidation reactions catalyzed by copper, zinc superoxide dismutase: intermediacy of carbonate anion radical J. Biol. Chem. 275 2000 14038 14045
    • (2000) J. Biol. Chem. , vol.275 , pp. 14038-14045
    • Zhang, H.1    Joseph, J.2    Felix, C.3    Kalyanaraman, B.4
  • 22
    • 0037059860 scopus 로고    scopus 로고
    • Bicarbonate enhances peroxidase activity of Cu,Zn-superoxide dismutase: Role of carbonate anion radical and scavenging of carbonate anion radical by metalloporphyrin antioxidant enzyme mimetics
    • H. Zhang, J. Joseph, M. Gurney, D. Becker, and B. Kalyanaraman Bicarbonate enhances peroxidase activity of Cu,Zn-superoxide dismutase: role of carbonate anion radical and scavenging of carbonate anion radical by metalloporphyrin antioxidant enzyme mimetics J. Biol. Chem. 277 2002 1013 1020
    • (2002) J. Biol. Chem. , vol.277 , pp. 1013-1020
    • Zhang, H.1    Joseph, J.2    Gurney, M.3    Becker, D.4    Kalyanaraman, B.5
  • 23
    • 0037929802 scopus 로고    scopus 로고
    • Bicarbonate dependent peroxidase activity of human Cu, Zn superoxide dismutase induces covalent aggregation of protein: Intermediacy of tryptophan-derived oxidation products
    • H. Zhang, C. Andrekopoulos, J. Joseph, K. Chandran, H. Karoui, J.P. Crow, and B. Kalyanaraman Bicarbonate dependent peroxidase activity of human Cu, Zn superoxide dismutase induces covalent aggregation of protein: intermediacy of tryptophan-derived oxidation products J. Biol. Chem. 278 2003 24078 24089
    • (2003) J. Biol. Chem. , vol.278 , pp. 24078-24089
    • Zhang, H.1    Andrekopoulos, C.2    Joseph, J.3    Chandran, K.4    Karoui, H.5    Crow, J.P.6    Kalyanaraman, B.7
  • 24
    • 0033214459 scopus 로고    scopus 로고
    • Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase: Role of carbonate anion radical
    • S.P.A. Goss, R.J. Singh, and B. Kalyanaraman Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase: role of carbonate anion radical J. Biol. Chem. 274 1999 28233 28239
    • (1999) J. Biol. Chem. , vol.274 , pp. 28233-28239
    • Goss, S.P.A.1    Singh, R.J.2    Kalyanaraman, B.3
  • 26
    • 0033520921 scopus 로고    scopus 로고
    • Evidence against the generation of free hydroxyl radicals from the interaction of copper,zinc-superoxide dismutase and hydrogen peroxide
    • S. Sankarapandi, and J.L. Zweier Evidence against the generation of free hydroxyl radicals from the interaction of copper,zinc-superoxide dismutase and hydrogen peroxide J. Biol. Chem. 274 1999 34576 34583
    • (1999) J. Biol. Chem. , vol.274 , pp. 34576-34583
    • Sankarapandi, S.1    Zweier, J.L.2
  • 27
    • 0035929681 scopus 로고    scopus 로고
    • - oxidoreductase and as a dichlorofluorescin peroxidase
    • - oxidoreductase and as a dichlorofluorescin peroxidase J. Biol. Chem. 276 2001 35253 35257
    • (2001) J. Biol. Chem. , vol.276 , pp. 35253-35257
    • Liochev, S.I.1    Fridovich, I.2
  • 29
    • 0015835435 scopus 로고
    • Rate constants for the reaction of the carbonate radical with compounds of biochemical interest in neutral aqueous solution
    • S.-N. Chen, and M.Z. Hoffman Rate constants for the reaction of the carbonate radical with compounds of biochemical interest in neutral aqueous solution Radiat. Res. 56 1973 40 47
    • (1973) Radiat. Res. , vol.56 , pp. 40-47
    • Chen, S.-N.1    Hoffman, M.Z.2
  • 30
  • 31
    • 0037376763 scopus 로고    scopus 로고
    • Immunochemical detection of hemoglobin-derived radicals formed by reaction with hydrogen peroxide: Involvement of a protein-tyrosyl radical
    • D.C. Ramirez, Y.-R. Chen, and R.P. Mason Immunochemical detection of hemoglobin-derived radicals formed by reaction with hydrogen peroxide: involvement of a protein-tyrosyl radical Free Radic. Biol. Med. 34 2003 830 839
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 830-839
    • Ramirez, D.C.1    Chen, Y.-R.2    Mason, R.P.3
  • 35
    • 0014691273 scopus 로고
    • The utility of superoxide dismutase in studying free radical reactions: I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen
    • J.M. McCord, and I. Fridovich The utility of superoxide dismutase in studying free radical reactions: I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen J. Biol. Chem. 244 1969 6056 6063
    • (1969) J. Biol. Chem. , vol.244 , pp. 6056-6063
    • McCord, J.M.1    Fridovich, I.2
  • 36
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
    • E.R. Stadtman Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences Free Radic. Biol. Med. 9 1990 315 325
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 37
    • 0026720020 scopus 로고
    • Direct evidence for inhibition of free radical formation from Cu(I) and hydrogen peroxide by glutathione and other potential ligands using the EPR spin-trapping technique
    • P.M. Hanna, and R.P. Mason Direct evidence for inhibition of free radical formation from Cu(I) and hydrogen peroxide by glutathione and other potential ligands using the EPR spin-trapping technique Arch. Biochem. Biophys. 295 1992 205 213
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 205-213
    • Hanna, P.M.1    Mason, R.P.2
  • 38
    • 0025344975 scopus 로고
    • 2 and ferric or cupric ions: Its modulation by histidine
    • 2 and ferric or cupric ions: its modulation by histidine Free Radic. Res. Commun. 9 1990 39 47
    • (1990) Free Radic. Res. Commun. , vol.9 , pp. 39-47
    • Tachon, P.1
  • 39
    • 0000174875 scopus 로고
    • New colorimetric reagent specific for copper: Determination of copper and iron
    • G. Smith, and D. Wilkins New colorimetric reagent specific for copper: determination of copper and iron Anal. Biochem. 25 1953 510 511
    • (1953) Anal. Biochem. , vol.25 , pp. 510-511
    • Smith, G.1    Wilkins, D.2
  • 40
    • 0037096201 scopus 로고    scopus 로고
    • Thiourea protects against copper-induced oxidative damage by formation of a redox-inactive thiourea-copper complex
    • B.-Z. Zhu, W.E. Antholine, and B. Frei Thiourea protects against copper-induced oxidative damage by formation of a redox-inactive thiourea-copper complex Free Radic. Biol. Med. 32 2002 1333 1338
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1333-1338
    • Zhu, B.-Z.1    Antholine, W.E.2    Frei, B.3
  • 42
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme
    • E.K. Hodgson, and I. Fridovich The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme Biochemistry 14 1975 5294 5299
    • (1975) Biochemistry , vol.14 , pp. 5294-5299
    • Hodgson, E.K.1    Fridovich, I.2
  • 44
    • 0025358959 scopus 로고
    • A. Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation
    • D.C. Salo, R.E. Pacifici, S.W. Lin, C. Giulivi, and K.J. Davies A. Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation J. Biol. Chem. 265 1990 11919 11927
    • (1990) J. Biol. Chem. , vol.265 , pp. 11919-11927
    • Salo, D.C.1    Pacifici, R.E.2    Lin, S.W.3    Giulivi, C.4    Davies, K.J.5
  • 45
    • 0024383765 scopus 로고
    • The interaction between Cu(I) superoxide dismutase and hydrogen peroxide
    • D.E. Cabelli, D. Allen, B.H.J. Bielski, and J. Holcman The interaction between Cu(I) superoxide dismutase and hydrogen peroxide J. Biol. Chem. 264 1989 9967 9971
    • (1989) J. Biol. Chem. , vol.264 , pp. 9967-9971
    • Cabelli, D.E.1    Allen, D.2    Bielski, B.H.J.3    Holcman, J.4
  • 46
    • 2342650119 scopus 로고    scopus 로고
    • 2 enhanced peroxidase activity of SOD1: The effects of pH
    • 2 enhanced peroxidase activity of SOD1: the effects of pH Free Radic. Biol. Med. 36 2004 1444 1447
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1444-1447
    • Liochev, S.I.1    Fridovich, I.2
  • 47
    • 0037088630 scopus 로고    scopus 로고
    • Histidinyl radical formation in the self-peroxidation reaction of bovine copper-zinc superoxide dismutase
    • M.R. Gunther, J.A. Peters, and M.K. Sivaneri Histidinyl radical formation in the self-peroxidation reaction of bovine copper-zinc superoxide dismutase J. Biol. Chem. 277 2002 9160 9166
    • (2002) J. Biol. Chem. , vol.277 , pp. 9160-9166
    • Gunther, M.R.1    Peters, J.A.2    Sivaneri, M.K.3
  • 48
    • 0033515433 scopus 로고    scopus 로고
    • Crystallographic structures of bovine copper,zinc superoxide dismutase reveal asymmetry in two subunits: Functionally important three and five coordinate copper sites captured in the same crystal
    • M.A. Hough, and S.S. Hasnain Crystallographic structures of bovine copper,zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal J. Mol. Biol. 287 1999 579 592
    • (1999) J. Mol. Biol. , vol.287 , pp. 579-592
    • Hough, M.A.1    Hasnain, S.S.2
  • 49
    • 0037375949 scopus 로고    scopus 로고
    • Reversal of the superoxide dismutase reaction revisited
    • S.I. Liochev, and I. Fridovich Reversal of the superoxide dismutase reaction revisited Free Radic. Biol. Med. 34 2003 908 910
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 908-910
    • Liochev, S.I.1    Fridovich, I.2
  • 51
    • 0028953264 scopus 로고
    • Reduction of copper, but not iron, by human low density lipoprotein (LDL): Implications for metal ion-dependent oxidative modification of LDL
    • S.M. Lynch, and B. Frei Reduction of copper, but not iron, by human low density lipoprotein (LDL): implications for metal ion-dependent oxidative modification of LDL J., Biol. Chem. 270 1995 5158 5163
    • (1995) J., Biol. Chem. , vol.270 , pp. 5158-5163
    • Lynch, S.M.1    Frei, B.2
  • 52
    • 0025954814 scopus 로고
    • Fenton chemistry: Amino acid oxidation
    • E.R. Stadtman, and B.S. Berlett Fenton chemistry: amino acid oxidation J. Biol. Chem. 266 1991 17201 17211
    • (1991) J. Biol. Chem. , vol.266 , pp. 17201-17211
    • Stadtman, E.R.1    Berlett, B.S.2
  • 53
    • 0028821559 scopus 로고
    • ESR evidence for the generation of reactive oxygen species from the copper-mediated oxidation of the benzene metabolite, hydroquinone: Role in DNA damage
    • Y. Li, P. Kuppusamy, J.L. Zweier, and M.A. Trush ESR evidence for the generation of reactive oxygen species from the copper-mediated oxidation of the benzene metabolite, hydroquinone: role in DNA damage Chem. Biol. Interact. 94 1995 101 120
    • (1995) Chem. Biol. Interact. , vol.94 , pp. 101-120
    • Li, Y.1    Kuppusamy, P.2    Zweier, J.L.3    Trush, M.A.4
  • 54
    • 0037087150 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein induced by the Cu,Zn-superoxide dismutase and hydrogen peroxide system
    • K.S. Kim, S.Y. Choi, H.Y. Kwon, M.H. Won, T.-C. Kang, and J.H. Kang Aggregation of alpha-synuclein induced by the Cu,Zn-superoxide dismutase and hydrogen peroxide system Free Radic. Biol. Med. 32 2002 544 550
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 544-550
    • Kim, K.S.1    Choi, S.Y.2    Kwon, H.Y.3    Won, M.H.4    Kang, T.-C.5    Kang, J.H.6
  • 55
    • 0002731550 scopus 로고    scopus 로고
    • Copper, zinc superoxide dismutase enhances DNA damage and mutagenicity induced by cysteine/iron
    • S.J. Yoon, Y.H. Koh, R.A. Floyd, and J.-W. Park Copper, zinc superoxide dismutase enhances DNA damage and mutagenicity induced by cysteine/iron Mutat. Res. 448 2000 97 104
    • (2000) Mutat. Res. , vol.448 , pp. 97-104
    • Yoon, S.J.1    Koh, Y.H.2    Floyd, R.A.3    Park, J.-W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.