메뉴 건너뛰기




Volumn 93, Issue 5, 2004, Pages 1122-1130

Selective Site-Specific Fenton Oxidation of Methionine in Model Peptides: Evidence for a Metal-Bound Oxidant

Author keywords

Fenton reaction; Met; Met sulfoxide; Reactive oxygen species

Indexed keywords

FERROUS ION; HYDROGEN PEROXIDE; METHIONINE; METHIONINE SULFOXIDE; OXIDIZING AGENT; PEPTIDE; REACTIVE OXYGEN METABOLITE;

EID: 1942498894     PISSN: 00223549     EISSN: None     Source Type: Journal    
DOI: 10.1002/jps.20013     Document Type: Article
Times cited : (19)

References (35)
  • 1
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins
    • Stadtman ER, Oliver CN. 1991. Metal-catalyzed oxidation of proteins. J Biol Chem 266:2005-2008.
    • (1991) J Biol Chem , vol.266 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 2
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. 1992. Protein oxidation and aging. Science 257:1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 3
    • 0023030789 scopus 로고
    • Sequence of a peptide susceptible to mixed-function oxidation
    • Farber JM, Levine RL. 1986. Sequence of a peptide susceptible to mixed-function oxidation. J Biol Chem 261:4574-4578.
    • (1986) J Biol Chem , vol.261 , pp. 4574-4578
    • Farber, J.M.1    Levine, R.L.2
  • 4
    • 0029028559 scopus 로고
    • Aggregation and precipitation of human relaxin induced by metal-catalyzed oxidation
    • Li S, Nguyen TH, Schöneich C, Borchardt RT. 1995. Aggregation and precipitation of human relaxin induced by metal-catalyzed oxidation. Biochemistry 34:5762-5772.
    • (1995) Biochemistry , vol.34 , pp. 5762-5772
    • Li, S.1    Nguyen, T.H.2    Schöneich, C.3    Borchardt, R.T.4
  • 5
    • 1842291518 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of histidine in human growth hormone: Mechanism, isotope effects, and inhibition by a mild denaturing alcohol
    • Zhao F, Ghezzo-Schöneich E, Aced GI, Milby T, Schöneich Ch. 1997. Metal-catalyzed oxidation of histidine in human growth hormone: Mechanism, isotope effects, and inhibition by a mild denaturing alcohol. J Biol Chem 272:9019-9029.
    • (1997) J Biol Chem , vol.272 , pp. 9019-9029
    • Zhao, F.1    Ghezzo-Schöneich, E.2    Aced, G.I.3    Milby, T.4    Schöneich, Ch.5
  • 6
    • 0027444875 scopus 로고
    • Iron-thiolate induced oxidation of Met to Met sulfoxide in small model peptides. Intramolecular catalysis by histidine
    • Schöneich Ch, Zhao F, Wilson GS, Borchardt RT. 1993. Iron-thiolate induced oxidation of Met to Met sulfoxide in small model peptides. Intramolecular catalysis by histidine. Biochim Biophys Acta 1158: 307-322.
    • (1993) Biochim Biophys Acta , vol.1158 , pp. 307-322
    • Schöneich, Ch.1    Zhao, F.2    Wilson, G.S.3    Borchardt, R.T.4
  • 8
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt W. 1995. Oxidation of methionyl residues in proteins: Tools, targets, and reversal. Free Radic Biol Med 18:93-105.
    • (1995) Free Radic Biol Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 9
    • 0028198779 scopus 로고
    • The Fenton oxidation mechanism: Reactivities of biologically relevant substrates with two oxidizing intermediates differ from those predicted for the hydroxyl radical
    • Wink DA, Nims RW, Saavedra JE, Utermahlen WE, Ford PC. 1994. The Fenton oxidation mechanism: Reactivities of biologically relevant substrates with two oxidizing intermediates differ from those predicted for the hydroxyl radical. Proc Natl Acad Sci USA 91:6604-6608.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6604-6608
    • Wink, D.A.1    Nims, R.W.2    Saavedra, J.E.3    Utermahlen, W.E.4    Ford, P.C.5
  • 10
    • 0026728425 scopus 로고
    • Formation of the excited ferryl species following Fenton reaction
    • Shen X, Tian J, Li J, Chen Y. 1992. Formation of the excited ferryl species following Fenton reaction. Free Radic Biol Med 13:585-592.
    • (1992) Free Radic Biol Med , vol.13 , pp. 585-592
    • Shen, X.1    Tian, J.2    Li, J.3    Chen, Y.4
  • 11
    • 0005955494 scopus 로고
    • EPR spin-trapping study on the oxidizing species formed in the reaction of the ferrous ion with hydrogen peroxide
    • Yamazaki I, Piette LH. 1991. EPR spin-trapping study on the oxidizing species formed in the reaction of the ferrous ion with hydrogen peroxide. J Am Chem Soc 113:7588-7593.
    • (1991) J Am Chem Soc , vol.113 , pp. 7588-7593
    • Yamazaki, I.1    Piette, L.H.2
  • 12
    • 0001368220 scopus 로고
    • +)] (1) as hydroxylases (RH→ROH), not as generators of free hydroxyl radicals (HO-)
    • +)] (1) as hydroxylases (RH→ROH), not as generators of free hydroxyl radicals (HO-). J Am Chem Soc 115:5817-5818.
    • (1993) J Am Chem Soc , vol.115 , pp. 5817-5818
    • Sawyer, D.T.1    Kang, C.2    Llobet, A.3    Redman, C.4
  • 13
    • 0022837916 scopus 로고
    • Oxidizing intermediates in the reaction of ferrous EDTA with hydrogen peroxide
    • Rush JD, Koppenol WH. 1986. Oxidizing intermediates in the reaction of ferrous EDTA with hydrogen peroxide. J Biol Chem 15:6730-6733.
    • (1986) J Biol Chem , vol.15 , pp. 6730-6733
    • Rush, J.D.1    Koppenol, W.H.2
  • 14
    • 0028327092 scopus 로고
    • Characteristics of an oxidant formed during iron (II) autoxidation
    • Reinke LA, Rau JM, McCay PB. 1994. Characteristics of an oxidant formed during iron (II) autoxidation. Free Radic Biol Med 16:485-492.
    • (1994) Free Radic Biol Med , vol.16 , pp. 485-492
    • Reinke, L.A.1    Rau, J.M.2    McCay, P.B.3
  • 15
    • 0000252108 scopus 로고
    • 2) in acetonitrile: Monoxygenation, dehydrogenations, and dioxygenations of organic substrates
    • 2) in acetonitrile: Monoxygenation, dehydrogenations, and dioxygenations of organic substrates. J Am Chem Soc 106:4283-4285.
    • (1984) J Am Chem Soc , vol.106 , pp. 4283-4285
    • Sugimoto, H.1    Sawyer, D.T.2
  • 16
    • 0025118364 scopus 로고
    • Synthesis and crystal and molecular structure of a conformationally restricted Met analogue
    • Glass RS, Hojjatie M, Sabahi M, Steffen LK, Wilson GS. 1990. Synthesis and crystal and molecular structure of a conformationally restricted Met analogue. J Org Chem 55:3797-3804.
    • (1990) J Org Chem , vol.55 , pp. 3797-3804
    • Glass, R.S.1    Hojjatie, M.2    Sabahi, M.3    Steffen, L.K.4    Wilson, G.S.5
  • 17
    • 0000097027 scopus 로고
    • Molecular design to mimic the copper(II) transport site of human albumin. The crystal and molecular structure of copper (II)-glycylglycyl-L-histidine N-methyl amide monoaquo complex
    • Camerman N, Camerman A, Sarkar B. 1976. Molecular design to mimic the copper(II) transport site of human albumin. The crystal and molecular structure of copper (II)-glycylglycyl-L-histidine N-methyl amide monoaquo complex. Can J Chem 54: 1309-1316.
    • (1976) Can J Chem , vol.54 , pp. 1309-1316
    • Camerman, N.1    Camerman, A.2    Sarkar, B.3
  • 18
    • 0039761298 scopus 로고
    • DNA modification: Intrinsic selectivity of nickel (II) complexes
    • Chen X, Rokita SE, Burrows CJ. 1991. DNA modification: Intrinsic selectivity of nickel (II) complexes. J Am Chem Soc 113:5884-5886.
    • (1991) J Am Chem Soc , vol.113 , pp. 5884-5886
    • Chen, X.1    Rokita, S.E.2    Burrows, C.J.3
  • 19
    • 0026795211 scopus 로고
    • Sequence-specific oxidative cleavage of DNA by a designed metalloprotein, Ni (II) GGH (Hin139-190)
    • Mack P, Dervan PB. 1992. Sequence-specific oxidative cleavage of DNA by a designed metalloprotein, Ni (II) GGH (Hin139-190). Biochemistry 31:9399-9405.
    • (1992) Biochemistry , vol.31 , pp. 9399-9405
    • Mack, P.1    Dervan, P.B.2
  • 20
    • 0000155173 scopus 로고
    • Design and synthesis of a versatile DNA-cleaving metallopeptide structural domain
    • Shullenberger DF, Eason PD, Long EC. 1993. Design and synthesis of a versatile DNA-cleaving metallopeptide structural domain. J Am Chem Soc 115:11038-11039.
    • (1993) J Am Chem Soc , vol.115 , pp. 11038-11039
    • Shullenberger, D.F.1    Eason, P.D.2    Long, E.C.3
  • 21
    • 0000609722 scopus 로고    scopus 로고
    • Oxidation of Met peptides by Fenton systems: The importance of peptide sequence, neighbouring groups, and EDTA
    • Schöneich Ch, Yang J. 1996. Oxidation of Met peptides by Fenton systems: The importance of peptide sequence, neighbouring groups, and EDTA. J Chem Soc Perkin Trans 2:915-924.
    • (1996) J Chem Soc Perkin Trans , vol.2 , pp. 915-924
    • Schöneich, Ch.1    Yang, J.2
  • 22
    • 0000505106 scopus 로고
    • Mechanism of oxidation of aliphatic thioethers to sulfoxides by hydroxyl radicals. The importance of molecular oxygen
    • Schöneich Ch, Aced A, Asmus K-D. 1993. Mechanism of oxidation of aliphatic thioethers to sulfoxides by hydroxyl radicals. The importance of molecular oxygen. J Am Chem Soc 115:11376-11383.
    • (1993) J Am Chem Soc , vol.115 , pp. 11376-11383
    • Schöneich, Ch.1    Aced, A.2    Asmus, K.-D.3
  • 23
    • 0028078034 scopus 로고
    • Side chain fragmentation of N-terminal threonine or serine residue induced through intramolecular proton transfer to hydroxy sulfuranyl radical formed at neighboring methionine in dipeptides
    • Schöneich Ch, Zhao F, Madden K-P, Bobrowski K. 1994. Side chain fragmentation of N-terminal threonine or serine residue induced through intramolecular proton transfer to hydroxy sulfuranyl radical formed at neighboring methionine in dipeptides. J Am Chem Soc 116:4641-4652.
    • (1994) J Am Chem Soc , vol.116 , pp. 4641-4652
    • Schöneich, Ch.1    Zhao, F.2    Madden, K.-P.3    Bobrowski, K.4
  • 24
    • 0025095792 scopus 로고
    • Site-specific oxidation of angiotensin I by copper (II) and L-ascorbate: Conversion of histidine residues to 2-imidazolones
    • Uchida K, Kawakishi S. 1990. Site-specific oxidation of angiotensin I by copper (II) and L-ascorbate: Conversion of histidine residues to 2-imidazolones. Arch Biochem Biophys 283:20-26.
    • (1990) Arch Biochem Biophys , vol.283 , pp. 20-26
    • Uchida, K.1    Kawakishi, S.2
  • 25
    • 0027368195 scopus 로고
    • 2-Oxo-histidine as a novel biological marker for oxidatively modified proteins
    • Uchida K, Kawakishi S. 1993. 2-Oxo-histidine as a novel biological marker for oxidatively modified proteins. FEBS Lett 332:208-210.
    • (1993) FEBS Lett , vol.332 , pp. 208-210
    • Uchida, K.1    Kawakishi, S.2
  • 26
    • 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. 269:2405-2410.
    • (1994) J Biol Chem , vol.269 , pp. 2405-2410
    • Uchida, K.1    Kawakishi, S.2
  • 27
    • 0028880110 scopus 로고
    • Determination of 2-oxohistidine by amino acid analysis
    • Lewisch SA, Levine RL. 1995. Determination of 2-oxohistidine by amino acid analysis. Anal Biochem 231:440-446.
    • (1995) Anal Biochem , vol.231 , pp. 440-446
    • Lewisch, S.A.1    Levine, R.L.2
  • 28
    • 0343986369 scopus 로고    scopus 로고
    • Mechanisms of metal-catalyzed oxidation of histidine to 2-oxo-histidine in peptides and proteins
    • Schöneich Ch. 2000. Mechanisms of metal-catalyzed oxidation of histidine to 2-oxo-histidine in peptides and proteins. J Pharm Biomed Anal 21: 1093-1097.
    • (2000) J Pharm Biomed Anal , vol.21 , pp. 1093-1097
    • Schöneich, Ch.1
  • 29
    • 0000936765 scopus 로고
    • Oxidation of amines and sulfides with hydrogen peroxide and alkyl hydrogen peroxide. The nature of the oxygen-transfer step
    • Bach RD, Su M-D, Schlegel B. 1994. Oxidation of amines and sulfides with hydrogen peroxide and alkyl hydrogen peroxide. The nature of the oxygen-transfer step. J Am Chem Soc 116:5379-5391.
    • (1994) J Am Chem Soc , vol.116 , pp. 5379-5391
    • Bach, R.D.1    Su, M.-D.2    Schlegel, B.3
  • 30
    • 0011194715 scopus 로고
    • Photochemical electron transfer involving 1,5-dithiacyclooctane. A recoverable charge relay in the photosensitized oxidation of halide
    • Jones G II, Malba V, Bergmark WR. 1986. Photochemical electron transfer involving 1,5-dithiacyclooctane. A recoverable charge relay in the photosensitized oxidation of halide. J Am Chem Soc 108:4214-4222.
    • (1986) J Am Chem Soc , vol.108 , pp. 4214-4222
    • Jones II, G.1    Malba, V.2    Bergmark, W.R.3
  • 31
    • 0342379061 scopus 로고
    • Anodic oxidation of diaryl sulfides I. Diphenyl sulphide in sulphate and perchlorate media
    • Houghton DS, Humffray AA. 1972. Anodic oxidation of diaryl sulfides I. Diphenyl sulphide in sulphate and perchlorate media. Electrochim Acta 17:1421-1433.
    • (1972) Electrochim Acta , vol.17 , pp. 1421-1433
    • Houghton, D.S.1    Humffray, A.A.2
  • 32
    • 0343189793 scopus 로고
    • Anodic oxidation of diaryl sulphides II. Diphenyl sulphide in halide media
    • Humffray AA, Houghton DS. 1972. Anodic oxidation of diaryl sulphides II. Diphenyl sulphide in halide media. Electrochim Acta 17:1435-1446.
    • (1972) Electrochim Acta , vol.17 , pp. 1435-1446
    • Humffray, A.A.1    Houghton, D.S.2
  • 33
    • 0027729733 scopus 로고
    • The development of stable protein formulation - A close look at protein aggregation, deamidation and oxidation
    • Cleland JL, Powell MF, Shire SJ. 1993. The development of stable protein formulation - A close look at protein aggregation, deamidation and oxidation. Crit Rev Ther Drug Carrier Syst 10:307-377.
    • (1993) Crit Rev Ther Drug Carrier Syst , vol.10 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 34
    • 0034103193 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of brain-derived neurotrophic factor (BDNF): Analytical challenges for the identification of modified sites
    • Jensen JL, Kolvenbach C, Roy S, Schöneich Ch. 2000. Metal-catalyzed oxidation of brain-derived neurotrophic factor (BDNF): Analytical challenges for the identification of modified sites. Pharm Res 17:190-196.
    • (2000) Pharm Res , vol.17 , pp. 190-196
    • Jensen, J.L.1    Kolvenbach, C.2    Roy, S.3    Schöneich, Ch.4
  • 35
    • 0034184529 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of brain-derived neurotrophic factor (BDNF): Selectivity and conformational consequences of histidine oxidation
    • Jensen JL, Kuczera K, Roy S, Schöneich Ch. 2000. Metal-catalyzed oxidation of brain-derived neurotrophic factor (BDNF): Selectivity and conformational consequences of histidine oxidation. Cell Mol Biol 46:685-696.
    • (2000) Cell Mol Biol , vol.46 , pp. 685-696
    • Jensen, J.L.1    Kuczera, K.2    Roy, S.3    Schöneich, Ch.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.