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Volumn 25, Issue 3-4, 2003, Pages 341-350

Peroxynitrite-dependent modifications of tyrosine residues in hemoglobin. Formation of tyrosyl radical(s) and 3-nitrotyrosine

Author keywords

Ferryl heme; Hemoglobin; Nitrotyrosine; Oxidative modification; Peroxynitrite; Tyrosine

Indexed keywords

3 NITROTYROSINE; CARBON DIOXIDE; CYTOCHROME; CYTOCHROME C; HEMOGLOBIN; HEMOPROTEIN; MANGANESE SUPEROXIDE DISMUTASE; METAL; METALLOPORPHYRIN; PEROXYNITRITE; SCAVENGER; SOLVENT; TYROSINE DERIVATIVE;

EID: 0347361495     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-003-0021-0     Document Type: Review
Times cited : (47)

References (89)
  • 2
    • 13144294985 scopus 로고    scopus 로고
    • Peroxynitrite-mediated heme oxidation and protein modification of native and chemically modified hemoglobins
    • Alayash AI, Brockner Ryan BA, Cashon RE (1998) Peroxynitrite-mediated heme oxidation and protein modification of native and chemically modified hemoglobins. Arch Biochem Biophys 349: 65-73
    • (1998) Arch Biochem Biophys , vol.349 , pp. 65-73
    • Alayash, A.I.1    Brockner Ryan, B.A.2    Cashon, R.E.3
  • 3
    • 0033534725 scopus 로고    scopus 로고
    • Kinetics of peroxynitrite reaction with amino acids and human serum albumin
    • Alvarez B, Ferrer-Sueta G, Freeman BA, Radi R (1999) Kinetics of peroxynitrite reaction with amino acids and human serum albumin. J Biol Chem 274: 842-848
    • (1999) J Biol Chem , vol.274 , pp. 842-848
    • Alvarez, B.1    Ferrer-Sueta, G.2    Freeman, B.A.3    Radi, R.4
  • 5
    • 0031408556 scopus 로고    scopus 로고
    • Catalysis of peroxynitrite reactions by manganese and iron porphyrins
    • Balavoine GG, Geletii YV, Bejan D (1997) Catalysis of peroxynitrite reactions by manganese and iron porphyrins. Nitric Oxide 1: 507-521
    • (1997) Nitric Oxide , vol.1 , pp. 507-521
    • Balavoine, G.G.1    Geletii, Y.V.2    Bejan, D.3
  • 6
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman BA (1990) Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA 87: 1620-1624
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 8
    • 0032539899 scopus 로고    scopus 로고
    • Carbon dioxide stimulates peroxynitrite-mediated nitration of tyrosine residues and inhibits oxidation of methionine residues of glutamine synthetase: Both modifications mimic effects of adenylylation
    • Berlett BS, Levine RL, Stadtman ER (1998) Carbon dioxide stimulates peroxynitrite-mediated nitration of tyrosine residues and inhibits oxidation of methionine residues of glutamine synthetase: both modifications mimic effects of adenylylation. Proc Natl Acad Sci USA 95: 2784-2789
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2784-2789
    • Berlett, B.S.1    Levine, R.L.2    Stadtman, E.R.3
  • 10
    • 0033574624 scopus 로고    scopus 로고
    • Direct EPR detection of carbonate radical anion produced from peroxynitrite and carbon dioxide
    • Bonini MG, Radi R, Ferrer-Sueta G, Ferriera AM, Augusto O (1999) Direct EPR detection of carbonate radical anion produced from peroxynitrite and carbon dioxide. J Biol Chem 274: 10802-10806
    • (1999) J Biol Chem , vol.274 , pp. 10802-10806
    • Bonini, M.G.1    Radi, R.2    Ferrer-Sueta, G.3    Ferriera, A.M.4    Augusto, O.5
  • 11
    • 0035971225 scopus 로고    scopus 로고
    • Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite
    • Bonini MG, Augusto O (2001) Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite. J Biol Chem 276: 9749-9754
    • (2001) J Biol Chem , vol.276 , pp. 9749-9754
    • Bonini, M.G.1    Augusto, O.2
  • 14
    • 0035146934 scopus 로고    scopus 로고
    • Nitric oxide, cytochrome-c oxidase and myoglobin
    • Brunori M (2001) Nitric oxide, cytochrome-c oxidase and myoglobin. Trends Biochem Sci 26: 21-23
    • (2001) Trends Biochem Sci , vol.26 , pp. 21-23
    • Brunori, M.1
  • 16
    • 0028090219 scopus 로고
    • Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide
    • Castro L, Rodriguez M, Radi R (1994) Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide. J Biol Chem 269: 29409-29415
    • (1994) J Biol Chem , vol.269 , pp. 29409-29415
    • Castro, L.1    Rodriguez, M.2    Radi, R.3
  • 17
    • 0015835435 scopus 로고
    • Rate constant for the reaction of carbonate radical with compounds of biochemical interest in neutral aqueous solution
    • Chen SN, Hoffman MZ (1973) Rate constant for the reaction of carbonate radical with compounds of biochemical interest in neutral aqueous solution. Radiat Res 56: 40-47
    • (1973) Radiat Res , vol.56 , pp. 40-47
    • Chen, S.N.1    Hoffman, M.Z.2
  • 18
    • 0034656837 scopus 로고    scopus 로고
    • Peroxynitrite scavenging by metalloporphyrins and thiolates
    • Crow JP (2000) Peroxynitrite scavenging by metalloporphyrins and thiolates. Free Radic Bio Med 28: 1487-1494
    • (2000) Free Radic Bio Med , vol.28 , pp. 1487-1494
    • Crow, J.P.1
  • 20
    • 1842289165 scopus 로고    scopus 로고
    • Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L
    • Crow JP, Ye Y-Z, Strong M, Kirk M, Barnes S, Beckman JS (1997) Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L. J Neurochem 69: 1945-1953
    • (1997) J Neurochem , vol.69 , pp. 1945-1953
    • Crow, J.P.1    Ye, Y.-Z.2    Strong, M.3    Kirk, M.4    Barnes, S.5    Beckman, J.S.6
  • 22
    • 0026063955 scopus 로고
    • Identification of a globin free radical in equine myoglobin treated with peroxides
    • Davies M (1991) Identification of a globin free radical in equine myoglobin treated with peroxides. Biochim Biophys Acta 1077: 86-90
    • (1991) Biochim Biophys Acta , vol.1077 , pp. 86-90
    • Davies, M.1
  • 23
    • 0030249458 scopus 로고    scopus 로고
    • Peroxynitrite reaction with carbon dioxide/bicarbonate: Kinetics and influence on peroxynitrite-mediated oxidations
    • Denicola A, Freeman BA, Trujillo M, Radi R (1996) Peroxynitrite reaction with carbon dioxide/bicarbonate: kinetics and influence on peroxynitrite- mediated oxidations. Arch Biochem Biophys 333: 49-58
    • (1996) Arch Biochem Biophys , vol.333 , pp. 49-58
    • Denicola, A.1    Freeman, B.A.2    Trujillo, M.3    Radi, R.4
  • 24
    • 0032584141 scopus 로고    scopus 로고
    • Diffusion of peroxynitrite across erythrocyte membranes
    • Denicola A, Souza JM, Radi R (1998) Diffusion of peroxynitrite across erythrocyte membranes. Proc Natl Acad Sci USA 95: 3566-3571
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3566-3571
    • Denicola, A.1    Souza, J.M.2    Radi, R.3
  • 25
    • 0034634543 scopus 로고    scopus 로고
    • Formation of compound I in the reaction of native myoglobins with hydrogen peroxide
    • Egawa T, Shimada H, Ishimura Y (2000) Formation of compound I in the reaction of native myoglobins with hydrogen peroxide. J Biol Chem 275: 34858-34866
    • (2000) J Biol Chem , vol.275 , pp. 34858-34866
    • Egawa, T.1    Shimada, H.2    Ishimura, Y.3
  • 28
    • 0034012164 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies of the peroxynitrite-mediated oxidation of oxymyoglobin and oxyhemoglobin
    • Exner M, Herold S (2000) Kinetic and mechanistic studies of the peroxynitrite-mediated oxidation of oxymyoglobin and oxyhemoglobin. Chem Res Toxicol 13: 287-293
    • (2000) Chem Res Toxicol , vol.13 , pp. 287-293
    • Exner, M.1    Herold, S.2
  • 29
    • 2642598048 scopus 로고    scopus 로고
    • Ternary copper complexes and manganese (III) tetrakis(4-benzoic acid) porphyrin catalyze peroxynitrite-dependent nitration of aromatics
    • Ferrer-Sueta G, Ruiz-Ramirez L, Radi R (1997) Ternary copper complexes and manganese (III) tetrakis(4-benzoic acid) porphyrin catalyze peroxynitrite-dependent nitration of aromatics. Chem Res Toxicol 10: 1338-1344
    • (1997) Chem Res Toxicol , vol.10 , pp. 1338-1344
    • Ferrer-Sueta, G.1    Ruiz-Ramirez, L.2    Radi, R.3
  • 30
    • 0344348820 scopus 로고    scopus 로고
    • Catalytic scavenging of peroxynitrite by isomeric Mn(III) N-methylpyridylporphyrins in the presence of reductants
    • Ferrer-Sueta G, Batinic'-Haberle I, Spasojevic' I, Fridovich I, Radi R (1999) Catalytic scavenging of peroxynitrite by isomeric Mn(III) N-methylpyridylporphyrins in the presence of reductants. Chem Res Toxicol 12: 442-449
    • (1999) Chem Res Toxicol , vol.12 , pp. 442-449
    • Ferrer-Sueta, G.1    Batinic'-Haberle, I.2    Spasojevic', I.3    Fridovich, I.4    Radi, R.5
  • 31
    • 0036122570 scopus 로고    scopus 로고
    • Reactions of manganese porphyrins and manganese-superoxide dismutase with peroxynitrite
    • Ferrer-Sueta G, Quijano C, Alvarez B, Radi R (2002) Reactions of manganese porphyrins and manganese-superoxide dismutase with peroxynitrite. Methods Enzymol 349: 23-37
    • (2002) Methods Enzymol , vol.349 , pp. 23-37
    • Ferrer-Sueta, G.1    Quijano, C.2    Alvarez, B.3    Radi, R.4
  • 33
    • 0027303364 scopus 로고
    • Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and catalase
    • Floris R, Piersma SR, Yang G, Jones P, Wever R (1993) Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and catalase. Eur J Biochem 215: 767-775
    • (1993) Eur J Biochem , vol.215 , pp. 767-775
    • Floris, R.1    Piersma, S.R.2    Yang, G.3    Jones, P.4    Wever, R.5
  • 34
    • 0031984429 scopus 로고    scopus 로고
    • Heme protein radicals: Formation, fate, and biological consequences
    • Giulivi C, Cadenas E (1998) Heme protein radicals: formation, fate, and biological consequences. Free Radic Biol Med 24: 269-279
    • (1998) Free Radic Biol Med , vol.24 , pp. 269-279
    • Giulivi, C.1    Cadenas, E.2
  • 35
    • 0032522210 scopus 로고    scopus 로고
    • 2: Evidence for carbonate radical production
    • 2: evidence for carbonate radical production. J Am Chem Soc 120: 3458-3463
    • (1998) J Am Chem Soc , vol.120 , pp. 3458-3463
    • Goldstein, S.1    Czapski, G.2
  • 36
    • 0030250041 scopus 로고    scopus 로고
    • Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration
    • Gow A, Duran D, Thom SR, Ischiropoulos H (1996a) Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration. Arch Biochem Biophys 333: 42-48
    • (1996) Arch Biochem Biophys , vol.333 , pp. 42-48
    • Gow, A.1    Duran, D.2    Thom, S.R.3    Ischiropoulos, H.4
  • 37
    • 0030002384 scopus 로고    scopus 로고
    • Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation
    • Gow AJ, Duran D, Malcom S, Ischiropoulos H (1996b) Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation. FEBS Lett 385: 63-66
    • (1996) FEBS Lett , vol.385 , pp. 63-66
    • Gow, A.J.1    Duran, D.2    Malcom, S.3    Ischiropoulos, H.4
  • 38
    • 0032171599 scopus 로고    scopus 로고
    • Modulation of leukocyte-endothelial interactions by reactive metabolites of oxygen and nitrogen: Relevance to ischemic heart disease
    • Grisham MB, Granger DN, Lefer DJ (1998) Modulation of leukocyte-endothelial interactions by reactive metabolites of oxygen and nitrogen: relevance to ischemic heart disease. Free Radic Biol Med 25: 404-433
    • (1998) Free Radic Biol Med , vol.25 , pp. 404-433
    • Grisham, M.B.1    Granger, D.N.2    Lefer, D.J.3
  • 39
    • 0030758774 scopus 로고    scopus 로고
    • Nitric oxide trapping of the tyrosyl radical of prostaglandin H synthase-2 leads to tyrosine iminoxyl radical and nitrotyrosine formation
    • Gunther MR, Hsi LC, Curtis JF, Gierse JK, Marnett LJ, Eling TE, Mason RP (1997) Nitric oxide trapping of the tyrosyl radical of prostaglandin H synthase-2 leads to tyrosine iminoxyl radical and nitrotyrosine formation. J Biol Chem 272: 17086-17090
    • (1997) J Biol Chem , vol.272 , pp. 17086-17090
    • Gunther, M.R.1    Hsi, L.C.2    Curtis, J.F.3    Gierse, J.K.4    Marnett, L.J.5    Eling, T.E.6    Mason, R.P.7
  • 41
    • 0028007172 scopus 로고
    • Quantitation of nitrotyrosine levels in lungs sections of patients and animals in acute lung injury
    • Haddad IY, Pataki G, Hu P, Galliani C, Beckman JS, Matalon S (1994) Quantitation of nitrotyrosine levels in lungs sections of patients and animals in acute lung injury. J Clin Invest 94: 2407-2413
    • (1994) J Clin Invest , vol.94 , pp. 2407-2413
    • Haddad, I.Y.1    Pataki, G.2    Hu, P.3    Galliani, C.4    Beckman, J.S.5    Matalon, S.6
  • 42
    • 0033046163 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of an intermediate peroxynitrite complex in the nitrogen monoxide induced oxidation of oxyhemoglobin
    • Herold S (1999) Kinetic and spectroscopic characterization of an intermediate peroxynitrite complex in the nitrogen monoxide induced oxidation of oxyhemoglobin. FEBS Lett 443: 81-84
    • (1999) FEBS Lett , vol.443 , pp. 81-84
    • Herold, S.1
  • 43
    • 0034794453 scopus 로고    scopus 로고
    • Peroxynitrite isomerization catalyzed by His64 myoglobin mutants
    • Herold S, Matsui T, Watanabe Y (2001) Peroxynitrite isomerization catalyzed by His64 myoglobin mutants. J Am Chem Soc 123: 4085-4086
    • (2001) J Am Chem Soc , vol.123 , pp. 4085-4086
    • Herold, S.1    Matsui, T.2    Watanabe, Y.3
  • 44
    • 0026172377 scopus 로고
    • Temperature dependence of the rate constants for the reaction of the carbonate radical with organic and inorganic reactants
    • Huie RE, Shoute LC, Neta P (1991) Temperature dependence of the rate constants for the reaction of the carbonate radical with organic and inorganic reactants. Int J Chem Kinet 23: 541-552
    • (1991) Int J Chem Kinet , vol.23 , pp. 541-552
    • Huie, R.E.1    Shoute, L.C.2    Neta, P.3
  • 45
    • 0036108894 scopus 로고    scopus 로고
    • Whence nitrotyrosine?
    • Hurst JK (2002) Whence nitrotyrosine? J Clin Invest 109: 1287-1289
    • (2002) J Clin Invest , vol.109 , pp. 1287-1289
    • Hurst, J.K.1
  • 47
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration - A pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos H (1998) Biological tyrosine nitration - a pathophysiological function of nitric oxide and reactive oxygen species. Arch Biochem Biophys 356: 1-11
    • (1998) Arch Biochem Biophys , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 48
    • 0027930057 scopus 로고
    • Evidence for nitric oxide-mediated oxidative damage in chronic inflammation. Nitrotyrosine in serum and synovial fluid from rheumatoid patients
    • Kaur H, Halliwell B (1994) Evidence for nitric oxide-mediated oxidative damage in chronic inflammation. Nitrotyrosine in serum and synovial fluid from rheumatoid patients. FEBS Lett 350: 9-12
    • (1994) FEBS Lett , vol.350 , pp. 9-12
    • Kaur, H.1    Halliwell, B.2
  • 49
    • 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
    • Kong S-K, Yim M, Stadman ER, Chock PB (1996) Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH2 peptide. Proc Natl Acad Sci USA 93: 3377-3382
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3377-3382
    • Kong, S.-K.1    Yim, M.2    Stadman, E.R.3    Chock, P.B.4
  • 50
    • 0025244380 scopus 로고
    • Acidic domains around nucleic acids
    • Lamm G, Pack GR (1990) Acidic domains around nucleic acids. Proc Natl Acad Sci USA 87: 9033-9036
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9033-9036
    • Lamm, G.1    Pack, G.R.2
  • 51
    • 0032486758 scopus 로고    scopus 로고
    • Mechanisms of iron porphyrins reactions with peroxynitrite
    • Lee JB, Hunt JA, Groves JT (1998a) Mechanisms of iron porphyrins reactions with peroxynitrite. J Am Chem Soc 120: 7493-7501
    • (1998) J Am Chem Soc , vol.120 , pp. 7493-7501
    • Lee, J.B.1    Hunt, J.A.2    Groves, J.T.3
  • 52
    • 0031750066 scopus 로고    scopus 로고
    • Manganese porphyrins as redox-couple peroxynitrite reductase
    • Lee JB, Hunt JA, Groves JT (1998b) Manganese porphyrins as redox-couple peroxynitrite reductase. J Am Chem Soc 120: 6053-6061
    • (1998) J Am Chem Soc , vol.120 , pp. 6053-6061
    • Lee, J.B.1    Hunt, J.A.2    Groves, J.T.3
  • 53
    • 0033567373 scopus 로고    scopus 로고
    • Radical mechanisms of the decomposition of peroxynitrite and the peroxynitrite-CO(2) adduct and of reactions with L-tyrosine and related compounds as studied by (15)N chemically induced dynamic nuclear polarization
    • Lehnig M (1999) Radical mechanisms of the decomposition of peroxynitrite and the peroxynitrite-CO(2) adduct and of reactions with L-tyrosine and related compounds as studied by (15)N chemically induced dynamic nuclear polarization. Arch Biochem Biophys 368: 303-318
    • (1999) Arch Biochem Biophys , vol.368 , pp. 303-318
    • Lehnig, M.1
  • 54
    • 0029680493 scopus 로고    scopus 로고
    • Carbon dioxide: Physiological catalyst for peroxynitrite-mediated cellular damage or cellular protectant?
    • Lymar SV, Hurst JK (1996) Carbon dioxide: physiological catalyst for peroxynitrite-mediated cellular damage or cellular protectant? Chem Res Toxicol 9: 845-850
    • (1996) Chem Res Toxicol , vol.9 , pp. 845-850
    • Lymar, S.V.1    Hurst, J.K.2
  • 55
    • 0029953744 scopus 로고    scopus 로고
    • Mechanism of carbon dioxide-catalyzed oxidation of tyrosine by peroxynitrite
    • Lymar SV, Jiang Q, Hurst JK (1996) Mechanism of carbon dioxide-catalyzed oxidation of tyrosine by peroxynitrite. Biochemistry 35: 7855-7861
    • (1996) Biochemistry , vol.35 , pp. 7855-7861
    • Lymar, S.V.1    Jiang, Q.2    Hurst, J.K.3
  • 56
    • 0033017612 scopus 로고    scopus 로고
    • A novel superoxide dismutase-based trap for peroxynitrite used to detect entry of peroxynitrite into erythrocyte ghosts
    • Macfadyen AJ, Reiter C, Zhuang Y, Beckman JS (1999) A novel superoxide dismutase-based trap for peroxynitrite used to detect entry of peroxynitrite into erythrocyte ghosts. Chem Res Toxicol 12: 223-229
    • (1999) Chem Res Toxicol , vol.12 , pp. 223-229
    • Macfadyen, A.J.1    Reiter, C.2    Zhuang, Y.3    Beckman, J.S.4
  • 57
    • 0032501998 scopus 로고    scopus 로고
    • Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and oxidation of critical tyrosine residues
    • MacMillan-Crow LA, Crow JP, Thompson JA (1998) Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and oxidation of critical tyrosine residues. Biochemistry 37: 1613-1622
    • (1998) Biochemistry , vol.37 , pp. 1613-1622
    • MacMillan-Crow, L.A.1    Crow, J.P.2    Thompson, J.A.3
  • 58
    • 0035902957 scopus 로고    scopus 로고
    • Nitrotyrosine mimics phosphotyrosine binding to the SH2 domain of the src family tyrosine kinase lyn
    • Mallozzi C, Di Stasi AMM, Minetti M (2001) Nitrotyrosine mimics phosphotyrosine binding to the SH2 domain of the src family tyrosine kinase lyn. FEBS Lett 503: 189-195
    • (2001) FEBS Lett , vol.503 , pp. 189-195
    • Mallozzi, C.1    Di Stasi, A.M.M.2    Minetti, M.3
  • 61
    • 0034682544 scopus 로고    scopus 로고
    • The decomposition of peroxynitrite does not yield nitroxyl anion and singlet oxygen
    • Merényi G, Lind J, Czapski G, Goldstein S (2000) The decomposition of peroxynitrite does not yield nitroxyl anion and singlet oxygen. Proc Natl Acad Sci USA 97: 8216-8218
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8216-8218
    • Merényi, G.1    Lind, J.2    Czapski, G.3    Goldstein, S.4
  • 63
    • 0034612336 scopus 로고    scopus 로고
    • Scavenging of peroxynitrite by oxyhemoglobin and identification of modified globin residues
    • Minetti M, Pietraforte D, Carbone V, Salzano AM, Scorza G, Marino G (2000) Scavenging of peroxynitrite by oxyhemoglobin and identification of modified globin residues. Biochemistry 39: 6689-6697
    • (2000) Biochemistry , vol.39 , pp. 6689-6697
    • Minetti, M.1    Pietraforte, D.2    Carbone, V.3    Salzano, A.M.4    Scorza, G.5    Marino, G.6
  • 65
    • 0014412965 scopus 로고
    • Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: The atomic model
    • Perutz MF, Muirhead H, Cox JM, Goaman LCG (1968) Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: the atomic model. Nature 219: 131-139
    • (1968) Nature , vol.219 , pp. 131-139
    • Perutz, M.F.1    Muirhead, H.2    Cox, J.M.3    Goaman, L.C.G.4
  • 66
    • 0031045787 scopus 로고    scopus 로고
    • One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: Evidence for the formation of protein tryptophan-centred radicals
    • Pietraforte D, Minetti M (1997a) One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: evidence for the formation of protein tryptophan-centred radicals. Biochem J 321: 734-750
    • (1997) Biochem J , vol.321 , pp. 734-750
    • Pietraforte, D.1    Minetti, M.2
  • 67
    • 0030814598 scopus 로고    scopus 로고
    • Direct ESR detection of peroxynitrite-induced tyrosine-centred protein radicals in human blood plasma
    • Pietraforte D, Minetti M (1997b) Direct ESR detection of peroxynitrite-induced tyrosine-centred protein radicals in human blood plasma. Biochem J 325: 675-684
    • (1997) Biochem J , vol.325 , pp. 675-684
    • Pietraforte, D.1    Minetti, M.2
  • 69
    • 0022426881 scopus 로고
    • Reactions of nitrogen dioxide in aqueous model systems: Oxidation of tyrosine units in peptides and proteins
    • Prutz WA, Monig H, Butler J, Land EJ (1986) Reactions of nitrogen dioxide in aqueous model systems: oxidation of tyrosine units in peptides and proteins. Arch Biochem Biophys 243: 125-134
    • (1986) Arch Biochem Biophys , vol.243 , pp. 125-134
    • Prutz, W.A.1    Monig, H.2    Butler, J.3    Land, E.J.4
  • 71
    • 0035853685 scopus 로고    scopus 로고
    • Reaction of peroxynitrite with Mn-superoxide dismutase: Role of the metal center in decomposition kinetics and nitration
    • Quijano C, Hernandez-Saavedra D, Castro L, Mc Cord JM, Freeman BA, Radi R (2001) Reaction of peroxynitrite with Mn-superoxide dismutase: role of the metal center in decomposition kinetics and nitration. J Biol Chem 276: 11631-11638
    • (2001) J Biol Chem , vol.276 , pp. 11631-11638
    • Quijano, C.1    Hernandez-Saavedra, D.2    Castro, L.3    Mc Cord, J.M.4    Freeman, B.A.5    Radi, R.6
  • 72
    • 0031826286 scopus 로고    scopus 로고
    • Peroxynitrite reactions and diffusion in biology
    • Radi R (1998) Peroxynitrite reactions and diffusion in biology. Chem Res Toxicol 11: 720-721
    • (1998) Chem Res Toxicol , vol.11 , pp. 720-721
    • Radi, R.1
  • 75
  • 77
    • 0034193163 scopus 로고    scopus 로고
    • Role of the carbonate radical anion in tyrosine nitration and hydroxylation by peroxynitrite
    • Santos CX, Bonini MG, Augusto O (2000) Role of the carbonate radical anion in tyrosine nitration and hydroxylation by peroxynitrite. Arch Biochem Biophys 377: 146-152
    • (2000) Arch Biochem Biophys , vol.377 , pp. 146-152
    • Santos, C.X.1    Bonini, M.G.2    Augusto, O.3
  • 78
    • 0028131242 scopus 로고
    • Reaction of peroxynitrite with oxyhaemoglobin: Interference with photometrical determination of nitric oxide
    • Schmidt K, Klatt P, Mayer B (1994) Reaction of peroxynitrite with oxyhaemoglobin: interference with photometrical determination of nitric oxide. Biochem J 301: 645-647
    • (1994) Biochem J , vol.301 , pp. 645-647
    • Schmidt, K.1    Klatt, P.2    Mayer, B.3
  • 79
    • 0032518743 scopus 로고    scopus 로고
    • One-electron oxidation pathway of thiols by peroxynitrite in biological fluids: Bicarbonate and ascorbate promote the formation of albumin disulphide dimers in human blood plasma
    • Scorza G, Minetti M (1998) One-electron oxidation pathway of thiols by peroxynitrite in biological fluids: bicarbonate and ascorbate promote the formation of albumin disulphide dimers in human blood plasma. Biochem J 329: 405-413
    • (1998) Biochem J , vol.329 , pp. 405-413
    • Scorza, G.1    Minetti, M.2
  • 80
    • 0014194993 scopus 로고
    • Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteins
    • Sokolovsky M, Riordan JF, Vallee BL (1967) Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteins. Biochem Biophys Res Commun 27: 20-25
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 20-25
    • Sokolovsky, M.1    Riordan, J.F.2    Vallee, B.L.3
  • 82
    • 0028977904 scopus 로고
    • +2 oxidation by peroxynitrite: Implications for superoxide measurements in nitric oxide-producing biological systems
    • +2 oxidation by peroxynitrite: implications for superoxide measurements in nitric oxide-producing biological systems. Arch Biochem Biophys 319: 491-497
    • (1995) Arch Biochem Biophys , vol.319 , pp. 491-497
    • Thomson, L.1    Truijllo, M.2    Telleri, R.3    Radi, R.4
  • 84
    • 0034078563 scopus 로고    scopus 로고
    • Increased nitrotyrosine staining in kidneys from patients with diabetic nephropathy
    • Thuraisingham RC, Nott CA, Dodd SM, Yaqoob MM (2000) Increased nitrotyrosine staining in kidneys from patients with diabetic nephropathy. Kidney Int 57: 1968-1972
    • (2000) Kidney Int , vol.57 , pp. 1968-1972
    • Thuraisingham, R.C.1    Nott, C.A.2    Dodd, S.M.3    Yaqoob, M.M.4
  • 85
    • 0029867717 scopus 로고    scopus 로고
    • Acceleration of peroxynitrite oxidations by carbon dioxide
    • Uppu RM, Squadrito GL, Pryor WA (1996) Acceleration of peroxynitrite oxidations by carbon dioxide. Arch Biochem Biophys 327: 335-343
    • (1996) Arch Biochem Biophys , vol.327 , pp. 335-343
    • Uppu, R.M.1    Squadrito, G.L.2    Pryor, W.A.3
  • 86
    • 0033564289 scopus 로고    scopus 로고
    • Protein modification during biological aging: Selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle
    • Viner RI, Ferrington DA, Williams TD, Bigelow DJ, Schoneich C (1999) Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle. Biochem J 340: 657-669
    • (1999) Biochem J , vol.340 , pp. 657-669
    • Viner, R.I.1    Ferrington, D.A.2    Williams, T.D.3    Bigelow, D.J.4    Schoneich, C.5
  • 87
    • 0028785105 scopus 로고
    • Formation of 8-nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination
    • Yermilov V, Rubio J, Ohshima H (1995) Formation of 8-nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination. FEBS Lett 376: 207-210
    • (1995) FEBS Lett , vol.376 , pp. 207-210
    • Yermilov, V.1    Rubio, J.2    Ohshima, H.3
  • 88
    • 0035954378 scopus 로고    scopus 로고
    • Nitration and oxidation of a hydrophobic tyrosine probe by peroxynitrite in membranes: Comparison with nitration and oxidation of tyrosine by peroxynitrite in aqueous solution
    • Zhang H, Joseph J, Feix J, Hogg N, Kalyanaraman B (2001) Nitration and oxidation of a hydrophobic tyrosine probe by peroxynitrite in membranes: comparison with nitration and oxidation of tyrosine by peroxynitrite in aqueous solution. Biochemistry 40: 7675-7686
    • (2001) Biochemistry , vol.40 , pp. 7675-7686
    • Zhang, H.1    Joseph, J.2    Feix, J.3    Hogg, N.4    Kalyanaraman, B.5
  • 89
    • 0034176278 scopus 로고    scopus 로고
    • Rapid reactions of peroxynitrite with heme-thiolate proteins as the basis for protection of prostacyclin synthase from inactivation by nitration
    • Zou MH, Daiber A, Shoun H, Peterson JA, Ullrich V (2000) Rapid reactions of peroxynitrite with heme-thiolate proteins as the basis for protection of prostacyclin synthase from inactivation by nitration. Arch Biochem Biophys 376: 149-155
    • (2000) Arch Biochem Biophys , vol.376 , pp. 149-155
    • Zou, M.H.1    Daiber, A.2    Shoun, H.3    Peterson, J.A.4    Ullrich, V.5


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