메뉴 건너뛰기




Volumn 13, Issue 6, 1996, Pages 931-938

Effects of polyaminocarboxylate mental chelators on iron-thiolate induced oxidation of methionine- and histidine-containing peptides

Author keywords

Chelator; Iron; Methionine histidine; Oxidation

Indexed keywords

CHELATING AGENT; EDETIC ACID; EGTAZIC ACID; ETHYLENEDIAMINE DERIVATIVE; HISTIDINE; HYDROGEN PEROXIDE; METHIONINE; NITRILOTRIACETIC ACID; PENTETIC ACID; SCAVENGER; AMMONIA; CARBOXYLIC ACID; CATALASE; FERRIC ION; IRON CHELATING AGENT; OLIGOPEPTIDE; REACTIVE OXYGEN METABOLITE; SULFOXIDE;

EID: 0029665540     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1016021716274     Document Type: Article
Times cited : (24)

References (31)
  • 1
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • E. R. Stadtman. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 62:797-821 (1993).
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 2
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins
    • E. R. Stadtman and C. N. Oliver. Metal-catalyzed oxidation of proteins. J. Biol. Chem. 266:2005-2008 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 3
    • 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 Rad. Biol. Med. 9:315-325 (1990).
    • (1990) Free Rad. Biol. Med. , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 5
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • W. Vogt. Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Rad. Biol. Med. 18:93-105 (1995).
    • (1995) Free Rad. Biol. Med. , vol.18 , pp. 93-105
    • Vogt, W.1
  • 6
    • 0029028559 scopus 로고
    • Aggregation and precipitation of human relaxin induced by metal-catalyzed oxidation
    • S. Li, T. Nguyen, C. Schöneich, and R. T. Borchardt. Aggregation and precipitation of human relaxin induced by metal-catalyzed oxidation. Biochemistry 34:5762-5772 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5762-5772
    • Li, S.1    Nguyen, T.2    Schöneich, C.3    Borchardt, R.T.4
  • 7
    • 0026546241 scopus 로고
    • Pharmaceutics of protein drugs
    • R. Pearlman and T. Nguyen. Pharmaceutics of protein drugs. J. Pharm. Pharmacol. 44(suppl.1): 178-185 (1992).
    • (1992) J. Pharm. Pharmacol. , vol.44 , Issue.1 SUPPL. , pp. 178-185
    • Pearlman, R.1    Nguyen, T.2
  • 8
    • 0023801411 scopus 로고
    • Isolation and characterization of a sulfoxide and a desamido derivative of biosynthetic human growth hormone
    • G. W. Becker, P. M. Tackitt, W. W. Bromer, D. S. Lefeber, and R. M. Riggin. Isolation and characterization of a sulfoxide and a desamido derivative of biosynthetic human growth hormone. Biotechnol. Appl. Biochem. 10:326-337 (1988).
    • (1988) Biotechnol. Appl. Biochem. , vol.10 , pp. 326-337
    • Becker, G.W.1    Tackitt, P.M.2    Bromer, W.W.3    Lefeber, D.S.4    Riggin, R.M.5
  • 9
    • 0025823103 scopus 로고
    • Dimerization of human growth hormone by zinc
    • B. C. Cunningham, M. G. Mulkerrin, J. A. Wells. Dimerization of human growth hormone by zinc. Science 253:545-548 (1991).
    • (1991) Science , vol.253 , pp. 545-548
    • Cunningham, B.C.1    Mulkerrin, M.G.2    Wells, J.A.3
  • 10
    • 0027444875 scopus 로고
    • Iron-thiolate induced oxidation of methionine to methionine sulfoxide in small model peptides. Intramolecular catalysis by histidine
    • Ch. Schöneich, F. Zhao, G. S. Wilson, and R. T. Borchardt. Iron-thiolate induced oxidation of methionine to methionine sulfoxide in small model peptides. Intramolecular catalysis by histidine. Biochim. Biophys. Acta 1158:307-322 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1158 , pp. 307-322
    • Schöneich, Ch.1    Zhao, F.2    Wilson, G.S.3    Borchardt, R.T.4
  • 12
    • 49249147345 scopus 로고
    • 31P relaxation rates of orthophosphate and ATP in the presence of EDTA. Evidence for EDTA-Fe(III)-phosphate ternary complexes
    • 31P relaxation rates of orthophosphate and ATP in the presence of EDTA. Evidence for EDTA-Fe(III)-phosphate ternary complexes. J. Magn. Reson. 36:147-150 (1979).
    • (1979) J. Magn. Reson. , vol.36 , pp. 147-150
    • Elgavish, G.A.1    Granot, J.2
  • 13
    • 0028057537 scopus 로고
    • Chromatographic separations of metal chelates present in commercial fertilizers. II. Development of an ion-pair chromatographic separation for the simultaneous determination of Fe(III) chelates of EDTA, DTPA, HEEDTA, EDDHA and EDDHMA, and the Cu(II), Zn(II) and Mn(II) chelates of EDTA
    • M. Deacon, M. R. Smyth, and L. G. M. T. Tuinstra. Chromatographic separations of metal chelates present in commercial fertilizers. II. Development of an ion-pair chromatographic separation for the simultaneous determination of Fe(III) chelates of EDTA, DTPA, HEEDTA, EDDHA and EDDHMA, and the Cu(II), Zn(II) and Mn(II) chelates of EDTA. J. Chromatog. A 659:349-357 (1994).
    • (1994) J. Chromatog. A , vol.659 , pp. 349-357
    • Deacon, M.1    Smyth, M.R.2    Tuinstra, L.G.M.T.3
  • 15
    • 0023060498 scopus 로고
    • Selective oxidation of imidazole ring in histidine residues by the ascorbic acid-copper ion system
    • K. Uchida and S. Kawakishi. Selective oxidation of imidazole ring in histidine residues by the ascorbic acid-copper ion system. Biochem. Biophys. Res. Commun. 138:659-665 (1986).
    • (1986) Biochem. Biophys. Res. Commun. , vol.138 , pp. 659-665
    • Uchida, K.1    Kawakishi, S.2
  • 16
    • 0021100174 scopus 로고
    • Oxidation modification of glutamine synthase
    • R. L. Levine. Oxidation modification of glutamine synthase. J. Biol. Chem. 258:11823-11827 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 11823-11827
    • Levine, R.L.1
  • 17
    • 0024447382 scopus 로고
    • Histidine and proline are important sites of free radical damage to proteins
    • R. T. Dean, S. P. Wolff, and M. A. McElligott. Histidine and proline are important sites of free radical damage to proteins. Free Rad. Res. Comms. 7:97-103 (1989).
    • (1989) Free Rad. Res. Comms. , vol.7 , pp. 97-103
    • Dean, R.T.1    Wolff, S.P.2    McElligott, M.A.3
  • 18
    • 0000302143 scopus 로고
    • Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins
    • W. M. Garrison. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem. Rev. 87:381-398 (1987).
    • (1987) Chem. Rev. , vol.87 , pp. 381-398
    • Garrison, W.M.1
  • 19
    • 37049101452 scopus 로고
    • III(edta)]-[edta=ethylenediaminetetra-acetate(4-)] catalyzed decomposition of hydrogen peroxide
    • III(edta)]-[edta=ethylenediaminetetra-acetate(4-)] catalyzed decomposition of hydrogen peroxide. J. Chem. Soc. Dalton Trans. 493-501 (1985).
    • (1985) J. Chem. Soc. Dalton Trans. , pp. 493-501
    • Francis, K.C.1    Cummins, D.2    Oakes, J.3
  • 20
    • 84918833988 scopus 로고
    • Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals in aqueous solution
    • G. V. Buxton, C. L. Greenstock, W. P. Helman, and A. B. Ross. Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals in aqueous solution. J. Phys. Chem. Ref. Data 17:513-886 (1988).
    • (1988) J. Phys. Chem. Ref. Data , vol.17 , pp. 513-886
    • Buxton, G.V.1    Greenstock, C.L.2    Helman, W.P.3    Ross, A.B.4
  • 21
    • 0023297560 scopus 로고
    • The reaction between ferrous polyaminocarboxylate complexes and hydrogen peroxide: An investigation of the reaction intermediates by stopped flow spectrophotometry
    • J. D. Rush and W. H. Koppenol. The reaction between ferrous polyaminocarboxylate complexes and hydrogen peroxide: an investigation of the reaction intermediates by stopped flow spectrophotometry. J. Inorg. Biochem. 29:199-215 (1987).
    • (1987) J. Inorg. Biochem. , vol.29 , pp. 199-215
    • Rush, J.D.1    Koppenol, W.H.2
  • 22
    • 0026566299 scopus 로고
    • Reaction of ferrous cytochrome c peroxidase with dioxygen: Site-directed mutagenesis provides evidence for rapid reduction of dioxygen by intramolecular electron transfer from the compound I radical site
    • M. A. Miller, D. Bandyopadyay, J. M. Mauro, T. G. Traylor, and J. Kraut. Reaction of ferrous cytochrome c peroxidase with dioxygen: site-directed mutagenesis provides evidence for rapid reduction of dioxygen by intramolecular electron transfer from the compound I radical site. Biochemistry 31:1992 (1992).
    • (1992) Biochemistry , vol.31 , pp. 1992
    • Miller, M.A.1    Bandyopadyay, D.2    Mauro, J.M.3    Traylor, T.G.4    Kraut, J.5
  • 23
    • 0001380631 scopus 로고
    • The reaction of superoxide radicalanion with dithiothreitol - A chain process
    • (a) N. Zhang, H. P. Schuchmann, and C. von Sonntag. The reaction of superoxide radicalanion with dithiothreitol - a chain process. J. Phys. Chem. 95:4718-4722 (1991).
    • (1991) J. Phys. Chem. , vol.95 , pp. 4718-4722
    • Zhang, N.1    Schuchmann, H.P.2    Von Sonntag, C.3
  • 24
    • 0344760994 scopus 로고
    • Chemistry of singlet oxygen-XXV. Photooxygenation of methionine
    • (b) P. K. Sysak, C. S. Foote, and Ta-Y. Ching. Chemistry of singlet oxygen-XXV. Photooxygenation of methionine. Photochem. Photobiol. 26:19-27 (1977)
    • (1977) Photochem. Photobiol. , vol.26 , pp. 19-27
    • Sysak, P.K.1    Foote, C.S.2    Ching, T.-Y.3
  • 25
    • 8944240771 scopus 로고    scopus 로고
    • calculated from catalase activity defined by Sigma
    • (c) calculated from catalase activity defined by Sigma.
  • 27
    • 0003385834 scopus 로고
    • The stereochemistry of the ethylenediamine-tetraacetatoaquoferrate(III) ion
    • J. L. Hoard, M. Lind, and J. V. Silverton. The stereochemistry of the ethylenediamine-tetraacetatoaquoferrate(III) ion. J. Am. Chem. Soc. 83:2770-2771 (1961).
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 2770-2771
    • Hoard, J.L.1    Lind, M.2    Silverton, J.V.3
  • 28
    • 0000505106 scopus 로고
    • Mechanism of oxidation of aliphatic thioethers to sulfoxides by hydroxyl radical. The importance of molecular oxygen
    • Ch. Schöneich, A. Aced, and K.-D. Asmus. Mechanism of oxidation of aliphatic thioethers to sulfoxides by hydroxyl radical. The importance of molecular oxygen. J. Am. Chem. Soc. 115:11376-11383 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11376-11383
    • Schöneich, Ch.1    Aced, A.2    Asmus, K.-D.3
  • 29
    • 0024012225 scopus 로고
    • Reduction of hydrogen peroxide by the ferrous iron chelate of diethylenetriamin-N,N,N′,N″,N″-pentaacetate
    • S. Rahhal and H. W. Richter. Reduction of hydrogen peroxide by the ferrous iron chelate of diethylenetriamin-N,N,N′,N″,N″-pentaacetate. J. Am. Chem. Soc. 110:3126-3133 (1988).
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 3126-3133
    • Rahhal, S.1    Richter, H.W.2
  • 30
    • 0000609722 scopus 로고    scopus 로고
    • Oxidation of methionine peptides by Fenton systems: The importance of peptide sequence, neighboring groups, and EDTA
    • in press
    • Ch. Schöneich and J. Yang. Oxidation of methionine peptides by Fenton systems: The importance of peptide sequence, neighboring groups, and EDTA. J. Chem. Soc. Perkin Trans II (1996), in press.
    • (1996) J. Chem. Soc. Perkin Trans II
    • Schöneich, Ch.1    Yang, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.