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Volumn 271, Issue 5, 2004, Pages 895-906

Mechanistic insight into the peroxidase catalyzed nitration of tyrosine derivatives by nitrite and hydrogen peroxide

Author keywords

Nitrogen dioxide; Peroxidases; Peroxynitrite; Phenol nitration; Reactive nitrogen species

Indexed keywords

HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; LACTOPEROXIDASE; NITRITE; NITROGEN DIOXIDE; PEROXIDASE; PEROXYNITRITE; TYROSINE DERIVATIVE;

EID: 1542314758     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.03992.x     Document Type: Article
Times cited : (58)

References (46)
  • 1
    • 0028362178 scopus 로고
    • Human exposure to oxides of nitrogen at ambient and supra-ambient concentrations
    • Mohsenin, V. (1994) Human exposure to oxides of nitrogen at ambient and supra-ambient concentrations. Toxicology 89, 301-312.
    • (1994) Toxicology , vol.89 , pp. 301-312
    • Mohsenin, V.1
  • 2
    • 0002496785 scopus 로고    scopus 로고
    • Biochemistry of nitric oxide and redox-related species
    • Feelisch, M. & Stamler, J.S., eds, Wiley, Chichester, UK
    • Stamler, J.S. & Feelisch, M. (1996) Biochemistry of nitric oxide and redox-related species. In Methods in Nitric Oxide Research (Feelisch, M. & Stamler, J.S., eds), pp. 19-27. Wiley, Chichester, UK.
    • (1996) Methods in Nitric Oxide Research , pp. 19-27
    • Stamler, J.S.1    Feelisch, M.2
  • 3
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada, S., Palmer, R.M.J. & Higgs, E.A. (1991) Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43, 109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 4
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and the ugly
    • Beckman, J.S. & Koppenol, W.H. (1996) Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and the ugly. Am. J. Physiol. 271, C1424-C1437.
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 5
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • Stamler, J.S., Lamas, S. & Fang, F.C. (2001) Nitrosylation: The prototypic redox-based signaling mechanism. Cell 106, 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 6
    • 0002880196 scopus 로고    scopus 로고
    • Metabolic fate of nitric oxide and related N-oxides
    • Feelisch, M. & Stamler, J.S., eds, Wiley, Chichester, UK
    • Kelm, M. & Yoshida, K. (1996) Metabolic fate of nitric oxide and related N-oxides. In Methods in Nitric Oxide Research (Feelisch, M. & Stamler, J.S., eds), pp. 47-58. Wiley, Chichester, UK.
    • (1996) Methods in Nitric Oxide Research , pp. 47-58
    • Kelm, M.1    Yoshida, K.2
  • 8
    • 0028827694 scopus 로고
    • Condensed expirate nitrite as a home marker for acute asthma
    • Hunt, J., Byrns, R.E., Ignarro, L.J. & Gaston, B. (1995) Condensed expirate nitrite as a home marker for acute asthma. Lancet 346, 1235-1236.
    • (1995) Lancet , vol.346 , pp. 1235-1236
    • Hunt, J.1    Byrns, R.E.2    Ignarro, L.J.3    Gaston, B.4
  • 9
    • 0027479429 scopus 로고
    • Reactive nitrogen intermediates and antimicrobial activity: Role of nitrite
    • Klebanoff, S.J. (1993) Reactive nitrogen intermediates and antimicrobial activity: role of nitrite. Free Radicals Biol. Med. 14, 351-360.
    • (1993) Free Radicals Biol. Med. , vol.14 , pp. 351-360
    • Klebanoff, S.J.1
  • 10
    • 0029760021 scopus 로고    scopus 로고
    • Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid. A novel mechanism for nitric oxide-mediated protein modification
    • Eiserich, J.P., Cross, C.E., Jones, A.D., Halliwell, B. & van der Vliet, A. (1996) Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid. A novel mechanism for nitric oxide-mediated protein modification. J. Biol. Chem. 271, 19199-19208.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19199-19208
    • Eiserich, J.P.1    Cross, C.E.2    Jones, A.D.3    Halliwell, B.4    Van Der Vliet, A.5
  • 11
    • 0029074616 scopus 로고
    • Degradation of chlorophyll by nitrogen dioxide generated from nitrite by the peroxidase reaction
    • Shibata, H., Kono, Y., Yamashita, S., Sawa, Y., Ochiai, H. & Tanaka, K. (1995) Degradation of chlorophyll by nitrogen dioxide generated from nitrite by the peroxidase reaction. Biochim. Biophys. Acta 1230, 45-50.
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 45-50
    • Shibata, H.1    Kono, Y.2    Yamashita, S.3    Sawa, Y.4    Ochiai, H.5    Tanaka, K.6
  • 12
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite
    • van der Vliet, A., Eiserich, J.P., Halliwell, B. & Cross, C.E. (1997) Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. J. Biol. Chem. 272, 7617-7625.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7617-7625
    • Van Der Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 13
    • 0032529412 scopus 로고    scopus 로고
    • Myeloperoxidase and horseradish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide
    • Sampson, J.B., Ye, Y.Z., Rosen, H. & Beckman, J.S. (1998) Myeloperoxidase and horseradish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide. Arch. Biochem. Biophys. 356, 207-213.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 207-213
    • Sampson, J.B.1    Ye, Y.Z.2    Rosen, H.3    Beckman, J.S.4
  • 16
    • 0035883152 scopus 로고    scopus 로고
    • N-15 Chemically induced dynamic nuclear polarization during reaction of N-acetyl-L-tyrosine with the nitrating systems nitrite/hydrogen peroxide/horseradish peroxidase and nitrite/hypochloric acid
    • Lehnig, M. (2001) N-15 Chemically induced dynamic nuclear polarization during reaction of N-acetyl-L-tyrosine with the nitrating systems nitrite/hydrogen peroxide/horseradish peroxidase and nitrite/hypochloric acid. Arch. Biochem. Biophys. 393, 245-254.
    • (2001) Arch. Biochem. Biophys. , vol.393 , pp. 245-254
    • Lehnig, M.1
  • 17
    • 0001057452 scopus 로고
    • Mechanism of action of peroxidases
    • Anni, H. & Yonetani, T. (1992) Mechanism of action of peroxidases. Met. Ions Biol. Syst. 28, 219-241.
    • (1992) Met. Ions Biol. Syst. , vol.28 , pp. 219-241
    • Anni, H.1    Yonetani, T.2
  • 19
    • 0029682870 scopus 로고    scopus 로고
    • Oxidative damage and tyrosine nitration from peroxynitrite
    • Beckman, J.S. (1996) Oxidative damage and tyrosine nitration from peroxynitrite. Chem. Res. Toxicol. 9, 836-844.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 836-844
    • Beckman, J.S.1
  • 20
    • 37049109925 scopus 로고
    • Electrophilic aromatic substitution. Part 21. Rate constants for formation of nitronium ion in aqueous sulfuric, perchloric, and methane-sulfonic acids
    • Moodie, R.B., Schofield, K. & Taylor, P.G. (1979) Electrophilic aromatic substitution. Part 21. Rate constants for formation of nitronium ion in aqueous sulfuric, perchloric, and methane-sulfonic acids. J. Chem. Soc. Perkin Trans. I 2, 133-136.
    • (1979) J. Chem. Soc. Perkin Trans. I , vol.2 , pp. 133-136
    • Moodie, R.B.1    Schofield, K.2    Taylor, P.G.3
  • 22
    • 0037124020 scopus 로고    scopus 로고
    • A tale of two controversies: Defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species
    • Brennan, M.-L., Wu, W., Fu, X., Shen, Z., Song, W., Frost, H., Vadseth, C., Narine, L., Lenkiewicz, E., Borchers, M.T., Lusis, A.J., Lee, J.J., Lee, N.A., Abu-Soud, H.M., Ischiropoulos, H. & Hazen, S.L. (2002) A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J. Biol. Chem. 277, 17415-17427.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17415-17427
    • Brennan, M.-L.1    Wu, W.2    Fu, X.3    Shen, Z.4    Song, W.5    Frost, H.6    Vadseth, C.7    Narine, L.8    Lenkiewicz, E.9    Borchers, M.T.10    Lusis, A.J.11    Lee, J.J.12    Lee, N.A.13    Abu-Soud, H.M.14    Ischiropoulos, H.15    Hazen, S.L.16
  • 24
    • 0029953744 scopus 로고    scopus 로고
    • Mechanism of carbon dioxide-catalyzed oxidation of tyrosine by peroxynitrite
    • Lymar, S.V., Jiang, Q. & Hurst, J.K. (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
  • 25
    • 0028361241 scopus 로고
    • The chloroperoxidase-catalyzed oxidation of phenols. Mechanism, selectivity, and characterization of enzyme-substrate complexes
    • Casella, L., Poli, S., Gullotti, M., Selvaggini, C., Beringhelli, T. & Marchesini, A. (1994) The chloroperoxidase-catalyzed oxidation of phenols. Mechanism, selectivity, and characterization of enzyme-substrate complexes. Biochemistry 33, 6377-6386.
    • (1994) Biochemistry , vol.33 , pp. 6377-6386
    • Casella, L.1    Poli, S.2    Gullotti, M.3    Selvaggini, C.4    Beringhelli, T.5    Marchesini, A.6
  • 27
    • 0031032436 scopus 로고    scopus 로고
    • Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover
    • Monzani, E., Gatti, A.L., Profumo, A., Casella, L. & Gullotti, M. (1997) Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover. Biochemistry 36, 1918-1926.
    • (1997) Biochemistry , vol.36 , pp. 1918-1926
    • Monzani, E.1    Gatti, A.L.2    Profumo, A.3    Casella, L.4    Gullotti, M.5
  • 28
    • 0028907862 scopus 로고
    • Spectroscopic investigations on the highly purified lactoperoxidase Fe(III)-heme catalytic site
    • Ferrari, R.P., Laurenti, E., Cecchini, P.I., Gambino, O. & Sondergaard, I. (1995) Spectroscopic investigations on the highly purified lactoperoxidase Fe(III)-heme catalytic site. J. Inorg. Biochem. 58, 109-127.
    • (1995) J. Inorg. Biochem. , vol.58 , pp. 109-127
    • Ferrari, R.P.1    Laurenti, E.2    Cecchini, P.I.3    Gambino, O.4    Sondergaard, I.5
  • 29
    • 37049135943 scopus 로고
    • Kinetics of decomposition of pernitrous acid
    • Hughes, M.N. & Nicklin, H.G. (1968) Kinetics of decomposition of pernitrous acid. J. Chem. Soc. 450-452.
    • (1968) J. Chem. Soc. , pp. 450-452
    • Hughes, M.N.1    Nicklin, H.G.2
  • 33
    • 0024291646 scopus 로고
    • On the reaction of ferric heme proteins with nitrite and sulfite
    • Young, L.J. & Siegel, L.M. (1988) On the reaction of ferric heme proteins with nitrite and sulfite. Biochemistry 27, 2790-2800.
    • (1988) Biochemistry , vol.27 , pp. 2790-2800
    • Young, L.J.1    Siegel, L.M.2
  • 35
    • 0033287895 scopus 로고    scopus 로고
    • Kinetic studies on the oxidation of nitrite by horseradish peroxidase and lactoperoxidase
    • Gebicka, L. (1999) Kinetic studies on the oxidation of nitrite by horseradish peroxidase and lactoperoxidase. Acta Biochim. Pol. 46, 919-927.
    • (1999) Acta Biochim. Pol. , vol.46 , pp. 919-927
    • Gebicka, L.1
  • 36
    • 0000660174 scopus 로고
    • Hammet pa correlation for reactions of lactoperoxidase compound II with phenols
    • Zhang, H. & Dunford, H.B. (1993) Hammet pa correlation for reactions of lactoperoxidase compound II with phenols. Can. J. Chem. 71, 1990-1994.
    • (1993) Can. J. Chem. , vol.71 , pp. 1990-1994
    • Zhang, H.1    Dunford, H.B.2
  • 37
    • 0022962952 scopus 로고
    • Hammett rho sigma correlation for reactions of horseradish peroxidase compound II with phenols
    • Dunford, H.B. & Adeniran, A.J. (1986) Hammett rho sigma correlation for reactions of horseradish peroxidase compound II with phenols. Arch. Biochem. Biophys. 251, 536-542.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 536-542
    • Dunford, H.B.1    Adeniran, A.J.2
  • 38
    • 0025240595 scopus 로고
    • Kinetic and molecular orbital studies on the rate of oxidation of mono-substituted phenols and anilines by horseradish peroxidase compound II
    • Sakurada, J., Sekiguchi, R., Sato, K. & Hosoya, T. (1990) Kinetic and molecular orbital studies on the rate of oxidation of mono-substituted phenols and anilines by horseradish peroxidase compound II. Biochemistry 29, 4093-4098.
    • (1990) Biochemistry , vol.29 , pp. 4093-4098
    • Sakurada, J.1    Sekiguchi, R.2    Sato, K.3    Hosoya, T.4
  • 39
    • 0030861053 scopus 로고    scopus 로고
    • Interpretation of the reactivity of peroxidase compounds I and II with phenols by the Marcus equation
    • Folkes, L.K. & Candeias, L.P. (1997) Interpretation of the reactivity of peroxidase compounds I and II with phenols by the Marcus equation. FEBS Lett. 412, 305-308.
    • (1997) FEBS Lett. , vol.412 , pp. 305-308
    • Folkes, L.K.1    Candeias, L.P.2
  • 40
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: A pathopysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos, H. (1998) Biological tyrosine nitration: a pathopysiological 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
  • 41
    • 0000996815 scopus 로고
    • Horseradish peroxidase. XII. Kinetic study of the oxidation of sulfite and nitrite by compounds I and II
    • Roman, R. & Dunford, H.B. (1973) Horseradish peroxidase. XII. Kinetic study of the oxidation of sulfite and nitrite by compounds I and II. Can. J. Chem. 51, 588-596.
    • (1973) Can. J. Chem. , vol.51 , pp. 588-596
    • Roman, R.1    Dunford, H.B.2
  • 42
    • 0017129482 scopus 로고
    • Substituent effect on the oxidation of phenols and aromatic amines by horseradish peroxidase compound I
    • Job, D. & Dunford, H.B. (1976) Substituent effect on the oxidation of phenols and aromatic amines by horseradish peroxidase compound I. Eur. J. Biochem. 66, 607-614.
    • (1976) Eur. J. Biochem. , vol.66 , pp. 607-614
    • Job, D.1    Dunford, H.B.2
  • 43
    • 0030939023 scopus 로고    scopus 로고
    • Kinetic studies on the oxidation of phenols by the horseradish peroxidase compound II
    • Patel, P.K., Mondal, M.S., Modi, S. & Behere, D.V. (1997) Kinetic studies on the oxidation of phenols by the horseradish peroxidase compound II. Biochim. Biophys. Acta 1339, 79-87.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 79-87
    • Patel, P.K.1    Mondal, M.S.2    Modi, S.3    Behere, D.V.4
  • 45
    • 0033231374 scopus 로고    scopus 로고
    • Manganese and iron porphyrins catalyze peroxynitrite decomposition and simultaneously increase nitration and oxidant yield: Implications for their use as peroxynitrite scavengers in vivo
    • Crow, J.P. (1999) Manganese and iron porphyrins catalyze peroxynitrite decomposition and simultaneously increase nitration and oxidant yield: Implications for their use as peroxynitrite scavengers in vivo. Arch. Biochem. Biophys. 371, 41-52.
    • (1999) Arch. Biochem. Biophys. , vol.371 , pp. 41-52
    • Crow, J.P.1
  • 46
    • 0033567373 scopus 로고    scopus 로고
    • 15N chemically induced dynamic nuclear polarization
    • 15N chemically induced dynamic nuclear polarization. Arch. Biochem. Biophys. 368, 303-318.
    • (1999) Arch. Biochem. Biophys. , vol.368 , pp. 303-318
    • Lehnig, M.1


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