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Volumn 26, Issue 7-8, 1999, Pages 905-918

A new look at a time-worn system: Oxidation of CuZn-SOD by H2O2

Author keywords

2 oxo histidine; Copper(I); Free radical; Hydrogen peroxide; Oxidation; Peptide fragmentation; Peroxidase activity; Superoxide dismutase

Indexed keywords

ARGON; COPPER ZINC SUPEROXIDE DISMUTASE; EDETIC ACID; FREE RADICAL; HYDROGEN PEROXIDE; PENTETIC ACID; PEROXIDASE;

EID: 0032921358     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(98)00274-3     Document Type: Article
Times cited : (70)

References (57)
  • 1
  • 2
    • 0015912256 scopus 로고
    • Pulse radiolytic investigations of superoxide catalyzed disproportionation. Mechanism for bovine superoxide dismutase
    • Klug-Roth D., Fridovich I., Rabani J. Pulse radiolytic investigations of superoxide catalyzed disproportionation. Mechanism for bovine superoxide dismutase. J. Am. Chem. Soc. 95:1973;2786-2790.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 2786-2790
    • Klug-Roth, D.1    Fridovich, I.2    Rabani, J.3
  • 3
    • 0015501473 scopus 로고
    • A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis
    • Klug D., Rabani J., Fridovich I. A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis. J. Biol. Chem. 247:1972;4839-4842.
    • (1972) J. Biol. Chem. , vol.247 , pp. 4839-4842
    • Klug, D.1    Rabani, J.2    Fridovich, I.3
  • 4
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme
    • Previous work by other investigators is reviewed in this paper
    • Hodgson, E. K.; Fridovich, I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 14:5294-5299; 1975. Previous work by other investigators is reviewed in this paper.
    • (1975) Biochemistry , vol.14 , pp. 5294-5299
    • Hodgson, E.K.1    Fridovich, I.2
  • 5
    • 0016816805 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Chemiluminescence and peroxidation
    • Hodgson E.K., Fridovich I. 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
  • 7
    • 0024277346 scopus 로고
    • 2 and Cu,Zn superoxide dismutase: Evidence for an electrostatic control of the reaction rate
    • 2 and Cu,Zn superoxide dismutase evidence for an electrostatic control of the reaction rate . Biochim. Biophys. Acta. 952:1988;77-82.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 77-82
    • Viglino, P.1    Scarpa, M.2    Rotilio, G.3    Rigo, A.4
  • 8
    • 0021104498 scopus 로고
    • -, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit
    • -, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase modification of one histidine per subunit . Arch. Biochem. Biophys. 224:1983;579-586.
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 579-586
    • Blech, D.M.1    Borders C.L., Jr.2
  • 10
    • 0015866291 scopus 로고
    • Observations on the oxidation-reduction properties of bovine erythrocyte superoxide dismutase
    • Fee J.A., DiCorleto P.E. Observations on the oxidation-reduction properties of bovine erythrocyte superoxide dismutase. Biochemistry. 12:1973;4893-4899.
    • (1973) Biochemistry , vol.12 , pp. 4893-4899
    • Fee, J.A.1    Dicorleto, P.E.2
  • 11
    • 0015921527 scopus 로고
    • On the mechanism of superoxide dismutase. Reaction of the bovine enzyme with hydrogen peroxide and ferrocyanide
    • Rotilio G., Morpurgo L., Calabrese L., Mondovi B. On the mechanism of superoxide dismutase. Reaction of the bovine enzyme with hydrogen peroxide and ferrocyanide. Biochim. Biophys. Acta. 302:1973;229-235.
    • (1973) Biochim. Biophys. Acta , vol.302 , pp. 229-235
    • Rotilio, G.1    Morpurgo, L.2    Calabrese, L.3    Mondovi, B.4
  • 13
    • 0025358959 scopus 로고
    • Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation
    • Salo D.C., Pacifici R.E., Lin S.W., Giulivi C., Davies K.J. 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
  • 14
    • 0026732669 scopus 로고
    • Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. Implication of reactive oxygen species
    • Ookawara T., Kawamura N., Kitagawa Y., Taniguchi N. Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. Implication of reactive oxygen species. J. Biol. Chem. 267:1992;18505-18510.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18505-18510
    • Ookawara, T.1    Kawamura, N.2    Kitagawa, Y.3    Taniguchi, N.4
  • 15
    • 0031592750 scopus 로고    scopus 로고
    • Fragmentation of human Cu,Zn-superoxide dismutase by peroxidative reaction
    • Kang J.H., Kim S.M. Fragmentation of human Cu,Zn-superoxide dismutase by peroxidative reaction. Mol. Cells. 7:1997;553-558.
    • (1997) Mol. Cells , vol.7 , pp. 553-558
    • Kang, J.H.1    Kim, S.M.2
  • 16
    • 0024376778 scopus 로고
    • Toward a Maillard reaction theory of aging
    • J.W. Baynes, Monnier V.M. New York: A. R. Liss
    • Monnier V.M. Toward a Maillard reaction theory of aging. Baynes J.W., Monnier V.M. Progress in clinical and biological research. Vol. 304:1989;1-22 A. R. Liss, New York.
    • (1989) Progress in Clinical and Biological Research , vol.304 , pp. 1-22
    • Monnier, V.M.1
  • 17
    • 0039743945 scopus 로고
    • Novel stabilization of a metalloprotein-ternary complex: Reaction of copper-zinc superoxide dismutase with diethyldithiocarbamate in polyacrylamide gels and its application to the study of the reaction of the dismutase with hydrogen peroxide
    • In: Rotilio, ed. Amsterdam: Elsevier Science
    • Jewett, S. L. Novel stabilization of a metalloprotein-ternary complex: reaction of copper-zinc superoxide dismutase with diethyldithiocarbamate in polyacrylamide gels and its application to the study of the reaction of the dismutase with hydrogen peroxide. In: Rotilio, ed. Superoxide and superoxide dismutase in chemistry, biology and medicine. Amsterdam: Elsevier Science; 1986: 178-180.
    • (1986) Superoxide and Superoxide Dismutase in Chemistry, Biology and Medicine , pp. 178-180
    • Jewett, S.L.1
  • 19
    • 0027368195 scopus 로고
    • 2-Oxo-histidine as a novel biological marker for oxidatively modified proteins
    • Uchida, K.; Kawakishi, S. 2-Oxo-histidine as a novel biological marker for oxidatively modified proteins. FEBS Lett. 332:208-210; 1993.
    • (1993) FEBS Lett. , vol.332 , pp. 208-210
    • Uchida, K.1    Kawakishi, S.2
  • 20
    • 0027980816 scopus 로고
    • 2. Selective generation of 2-oxo-histidine at histidine-118
    • 2. Selective generation of 2-oxo-histidine at histidine-118. J. Biol. Chem. 269:1994;2405-2410.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2405-2410
    • Uchida, K.1    Kawakishi, S.2
  • 21
    • 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
  • 22
    • 0017815770 scopus 로고
    • Considerations in the spin trapping of superoxide and hydroxyl radical in aqueous systems using 5,5′-dimethyl-1-pyrroline-1-oxide
    • Buettner G.R., Oberley L.W. Considerations in the spin trapping of superoxide and hydroxyl radical in aqueous systems using 5,5′-dimethyl-1-pyrroline-1-oxide. Biochem. Biophys. Res. Commun. 83:1978;69-74.
    • (1978) Biochem. Biophys. Res. Commun. , vol.83 , pp. 69-74
    • Buettner, G.R.1    Oberley, L.W.2
  • 23
    • 0015523099 scopus 로고
    • The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase
    • Misra H.P., Fridovich I. The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J. Biol. Chem. 47:1972;3170-3175.
    • (1972) J. Biol. Chem. , vol.47 , pp. 3170-3175
    • Misra, H.P.1    Fridovich, I.2
  • 24
    • 0017139230 scopus 로고
    • A sensitive assay for superoxide dismutase based on the autoxidation of 6-hydroxydopamine
    • Heikkila R.E., Cabbat F. A sensitive assay for superoxide dismutase based on the autoxidation of 6-hydroxydopamine. Anal. Biochem. 75:1976;356-362.
    • (1976) Anal. Biochem. , vol.75 , pp. 356-362
    • Heikkila, R.E.1    Cabbat, F.2
  • 25
    • 0027259236 scopus 로고
    • Variation of one unit of activity with oxidation rate of organic substrate in indirect superoxide dismutase assays
    • Jewett S.L., Rocklin A.M. Variation of one unit of activity with oxidation rate of organic substrate in indirect superoxide dismutase assays. Anal. Biochem. 212:1993;555-559.
    • (1993) Anal. Biochem. , vol.212 , pp. 555-559
    • Jewett, S.L.1    Rocklin, A.M.2
  • 26
    • 0015520583 scopus 로고
    • Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase
    • Rotilio G., Calabrese L., Bossa F., Barra D., Agrò A.F., Mondovi B. Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase. Biochemistry. 11:1972;2182-2187.
    • (1972) Biochemistry , vol.11 , pp. 2182-2187
    • Rotilio, G.1    Calabrese, L.2    Bossa, F.3    Barra, D.4    Agrò, A.F.5    Mondovi, B.6
  • 29
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244:1969;4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 30
    • 0017740440 scopus 로고
    • A new staining technique for proteins in polyacrylamide gels using Coomassie brilliant blue G-250
    • Blakesley W.R., Boezi J.A. A new staining technique for proteins in polyacrylamide gels using Coomassie brilliant blue G-250. Anal. Biochem. 82:1977;580-582.
    • (1977) Anal. Biochem. , vol.82 , pp. 580-582
    • Blakesley, W.R.1    Boezi, J.A.2
  • 31
    • 2042486710 scopus 로고
    • Spectroelectrochemistry of copper-zinc superoxide dismutase
    • St. Clair C.S., Gray H.B., Valentine J.S. Spectroelectrochemistry of copper-zinc superoxide dismutase. Inorg. Chem. 31:1992;925-927.
    • (1992) Inorg. Chem. , vol.31 , pp. 925-927
    • St. Clair, C.S.1    Gray, H.B.2    Valentine, J.S.3
  • 32
    • 0004052075 scopus 로고
    • New York: Oxford University Press
    • Sawyer D.T. Oxygen Chemistry. 1991;21 Oxford University Press, New York.
    • (1991) Oxygen Chemistry , pp. 21
    • Sawyer, D.T.1
  • 33
    • 0018786876 scopus 로고
    • Potentiometric titrations and oxidation-reduction potentials of manganese and copper-zinc superoxide dismutases
    • Lawrence G.D., Sawyer D.T. Potentiometric titrations and oxidation-reduction potentials of manganese and copper-zinc superoxide dismutases. Biochemistry. 18:1979;3045-3050.
    • (1979) Biochemistry , vol.18 , pp. 3045-3050
    • Lawrence, G.D.1    Sawyer, D.T.2
  • 34
    • 0000013089 scopus 로고
    • Evidence of the breaking of the copper-imidazolate bridge in copper/cobalt-substituted superoxide dismutase upon reduction of the copper(II) centers
    • Bertini I., Luchinat C., Monnanni R. Evidence of the breaking of the copper-imidazolate bridge in copper/cobalt-substituted superoxide dismutase upon reduction of the copper(II) centers. J. Am. Chem. Soc. 107:1985;2178-2179.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2178-2179
    • Bertini, I.1    Luchinat, C.2    Monnanni, R.3
  • 37
    • 0000153938 scopus 로고
    • The dissociation constants of some alkyl and acyl hydroperoxides
    • Everett A.J., Minkoff G.J. The dissociation constants of some alkyl and acyl hydroperoxides. Trans. Faraday Soc. 49:1953;410-414.
    • (1953) Trans. Faraday Soc. , vol.49 , pp. 410-414
    • Everett, A.J.1    Minkoff, G.J.2
  • 40
    • 0006474911 scopus 로고
    • Oxidation of tertiary amine buffers by copper(II)
    • Wang F., Sayre L.M. Oxidation of tertiary amine buffers by copper(II). Inorg. Chem. 28:1989;169-170.
    • (1989) Inorg. Chem. , vol.28 , pp. 169-170
    • Wang, F.1    Sayre, L.M.2
  • 41
    • 0242476277 scopus 로고
    • 4- reduction of a sterically constrained bis(substituted phenanthroline) complex of copper(II) in aqueous solution
    • 4- reduction of a sterically constrained bis(substituted phenanthroline) complex of copper(II) in aqueous solution. Inorg. Chem. 20:1981;1466-1469.
    • (1981) Inorg. Chem. , vol.20 , pp. 1466-1469
    • Al-Shatti, N.1    Lappin, A.G.2    Sykes, A.G.3
  • 44
    • 0038844990 scopus 로고
    • Copper-mediated nitrogen ligand oxidation and oxygenation
    • K.D. Karlin, & Z. Tyeklár. New York: Chapman and Hall
    • Sayre L.M., Tang W., Reedy K.V., Nadkarni D. Copper-mediated nitrogen ligand oxidation and oxygenation. Karlin K.D., Tyeklár Z. Bioinorganic chemistry of copper. 1993;236-248 Chapman and Hall, New York.
    • (1993) Bioinorganic Chemistry of Copper , pp. 236-248
    • Sayre, L.M.1    Tang, W.2    Reedy, K.V.3    Nadkarni, D.4
  • 45
    • 85050430651 scopus 로고
    • Binding and activation of molecular oxygen by copper complexes
    • S.J. Lippard. New York: John Wiley and Sons
    • Karlin K.D., Gultneh Y. Binding and activation of molecular oxygen by copper complexes. Lippard S.J. Progress in inorganic chemistry. 1987;219-327 John Wiley and Sons, New York.
    • (1987) Progress in Inorganic Chemistry , pp. 219-327
    • Karlin, K.D.1    Gultneh, Y.2
  • 46
    • 0025297079 scopus 로고
    • Highly site-specific oxygenation of 1-methylhistidine and its analogue with a copper(II)/ascorbate-dependent redox system
    • Uchida K., Kawakishi S. Highly site-specific oxygenation of 1-methylhistidine and its analogue with a copper(II)/ascorbate-dependent redox system. Biochim. Biophys. Acta. 1034:1990;347-350.
    • (1990) Biochim. Biophys. Acta , vol.1034 , pp. 347-350
    • Uchida, K.1    Kawakishi, S.2
  • 47
    • 0025285382 scopus 로고
    • Copper,zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide
    • Yim M.B., Chock P.B., Stadtman E.R. Copper,zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proc. Natl. Acad. Sci. USA. 87:1990;5006-5010.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5006-5010
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 48
    • 0027456505 scopus 로고
    • Enzyme function of copper,zinc superoxide dismutase as a free radical generator
    • Yim M.B., Chock P.B., Stadtman E.R. 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
  • 49
  • 52
    • 0029939471 scopus 로고    scopus 로고
    • A gain-of-function of an amyotropic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to an decrease in Km for hydrogen peroxide
    • Yim M.B., Kang J.-H., Yim Y.-S., Kwak H.-S., Chock P.B., Stadtman E.R. A gain-of-function of an amyotropic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant an enhancement of free radical formation due to an decrease in Km for hydrogen peroxide . Proc. Natl. Acad. Sci. USA. 93:1996;5709-5714.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 5709-5714
    • Yim, M.B.1    Kang, J.-H.2    Yim, Y.-S.3    Kwak, H.-S.4    Chock, P.B.5    Stadtman, E.R.6
  • 56
    • 0028950523 scopus 로고
    • Reactions of copper(II)-oligopeptide complexes with hydrogen peroxide: Effect of biological reductants
    • Ueda J.I., Shimazu Y., Ozawa T. Reactions of copper(II)-oligopeptide complexes with hydrogen peroxide effect of biological reductants . Free Radic. Biol. Med. 18:1995;929-933.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 929-933
    • Ueda, J.I.1    Shimazu, Y.2    Ozawa, T.3
  • 57
    • 0026577698 scopus 로고
    • Reactions of copper(II)-N-polycarboxylate complexes and hydrogen peroxide in the presence of biological reductants: ESR evidence for hydroxyl radicals
    • Ozawa T., Hanaki A., Onodera K., Kasai M. Reactions of copper(II)-N-polycarboxylate complexes and hydrogen peroxide in the presence of biological reductants ESR evidence for hydroxyl radicals . Biochem. Int. 26:1992;477-483.
    • (1992) Biochem. Int. , vol.26 , pp. 477-483
    • Ozawa, T.1    Hanaki, A.2    Onodera, K.3    Kasai, M.4


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