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Volumn 43, Issue 51, 2004, Pages 16393-16404

Mechanistic studies of the oxidation of oxyhemoglobin by peroxynitrite

Author keywords

[No Author keywords available]

Indexed keywords

NITRATES; NITROGEN OXIDES; OXIDATION; RATE CONSTANTS;

EID: 11144298023     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0482250     Document Type: Article
Times cited : (51)

References (55)
  • 1
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., and Freeman, B. A. (1990) Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide, Proc. Natl. Acad. Sci. U.S.A. 87, 1620-1624.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 2
    • 0037172177 scopus 로고    scopus 로고
    • The rate constant of the reaction of Superoxide with nitrogen monoxide: Approaching the diffusion limit
    • Nauser, T., and Koppenol, W. H. (2002) The rate constant of the reaction of Superoxide with nitrogen monoxide: Approaching the diffusion limit, J. Phys. Chem. A. 106, 4084-4086.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 4084-4086
    • Nauser, T.1    Koppenol, W.H.2
  • 3
    • 0027303364 scopus 로고
    • Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and catalase
    • Floris, R., Piersma, S. R., Yang, G., Jones, P., and 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
  • 4
    • 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    Trujillo, M.2    Telleri, R.3    Radi, R.4
  • 6
    • 0037371492 scopus 로고    scopus 로고
    • Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin
    • Herold, S., and Rehmann, F.-J. K. (2003) Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin, Free Radical Biol. Med. 34, 531-545.
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 531-545
    • Herold, S.1    Rehmann, F.-J.K.2
  • 7
    • 3042771981 scopus 로고    scopus 로고
    • Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants
    • Herold, S., Shivashankar, K., Matsui, T., and Watanabe, Y. (2004) Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants, J. Am. Chem. Soc. 126, 6945-6955.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6945-6955
    • Herold, S.1    Shivashankar, K.2    Matsui, T.3    Watanabe, Y.4
  • 8
    • 0033678831 scopus 로고    scopus 로고
    • Nitration and activation of cytochrome P450BM-3 by peroxynitrite. Stopped-flow measurements prove ferryl intermediates
    • Daiber, A., Herold, S., Schöneich, C., Namgaladze, D., Peterson, J. A., and Ullrich, V. (2000) Nitration and activation of cytochrome P450BM-3 by peroxynitrite. Stopped-flow measurements prove ferryl intermediates, Eur. J. Biochem. 267, 6729-6739.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6729-6739
    • Daiber, A.1    Herold, S.2    Schöneich, C.3    Namgaladze, D.4    Peterson, J.A.5    Ullrich, V.6
  • 9
    • 11944262823 scopus 로고
    • Rapid reaction between peroxynitrite ion and carbon dioxide: Implications for biological activity
    • Lymar, S. V., and Hurst, J. K. (1995) Rapid reaction between peroxynitrite ion and carbon dioxide: Implications for biological activity, J. Am. Chem. Soc. 117, 8867-8868.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8867-8868
    • Lymar, S.V.1    Hurst, J.K.2
  • 10
    • 0030249458 scopus 로고    scopus 로고
    • Peroxynitrite reaction with carbon dioxide/bicarbonate: Kinetics and influence on peroxynitrite-mediated oxidations
    • Denicola, A., Freeman, B. A., Trujillo, M., and 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
  • 11
    • 2942756048 scopus 로고    scopus 로고
    • The outer-sphere oxidation of nitrosyliron(II)-hemoglobin by peroxynitrite leads to the release of nitrogen monoxide
    • Herold, S. (2004) The outer-sphere oxidation of nitrosyliron(II)- hemoglobin by peroxynitrite leads to the release of nitrogen monoxide, Inorg. Chem. 43, 3783-3785.
    • (2004) Inorg. Chem. , vol.43 , pp. 3783-3785
    • Herold, S.1
  • 12
    • 0034012164 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies of the peroxynitrite-mediated oxidation of oxymyoglobin and oxyhemoglobin
    • Exner, M., and 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
  • 13
    • 0037348406 scopus 로고    scopus 로고
    • The mechanism of the peroxynitrite-mediated oxidation of myoglobin in the absence and in the presence of carbon dioxide
    • Herold, S., Exner, M., and Boccini, F. (2003) The mechanism of the peroxynitrite-mediated oxidation of myoglobin in the absence and in the presence of carbon dioxide, Chem. Res. Toxicol. 16, 390-402.
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 390-402
    • Herold, S.1    Exner, M.2    Boccini, F.3
  • 14
    • 0032584141 scopus 로고    scopus 로고
    • Diffusion of peroxynitrite across erythrocyte membranes
    • Denicola, A., Souza, J. M., and Radi, R. (1998) Diffusion of peroxynitrite across erythrocyte membranes, Proc. Natl. Acad. Sci. U.S.A. 95, 3566-3571.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3566-3571
    • Denicola, A.1    Souza, J.M.2    Radi, R.3
  • 15
    • 0033179574 scopus 로고    scopus 로고
    • Diffusion of peroxynitrite in the presence of carbon dioxide
    • Romero, N., Denicola, A., Souza, J. M., and Radi, R. (1999) Diffusion of peroxynitrite in the presence of carbon dioxide, Arch. Biochem. Biophys. 368, 23-30.
    • (1999) Arch. Biochem. Biophys. , vol.368 , pp. 23-30
    • Romero, N.1    Denicola, A.2    Souza, J.M.3    Radi, R.4
  • 16
    • 0029834589 scopus 로고    scopus 로고
    • Syntheses of peroxynitrite: To go with the flow or on solid grounds?
    • Koppenol, W. H., Kissner, R., and Beckman, J. S. (1996) Syntheses of peroxynitrite: to go with the flow or on solid grounds? Methods Enzymol. 269, 296-302.
    • (1996) Methods Enzymol. , vol.269 , pp. 296-302
    • Koppenol, W.H.1    Kissner, R.2    Beckman, J.S.3
  • 17
    • 0020473987 scopus 로고
    • Mechanism of autocatalytic oxidation of oxyhemoglobin by nitrite. An intermediate detected by electron spin resonance
    • Kosaka, H., Imaizumi, K., and Tyuma, I. (1982) Mechanism of autocatalytic oxidation of oxyhemoglobin by nitrite. An intermediate detected by electron spin resonance, Biochim. Biophys. Acta 702, 237-241.
    • (1982) Biochim. Biophys. Acta , vol.702 , pp. 237-241
    • Kosaka, H.1    Imaizumi, K.2    Tyuma, I.3
  • 19
    • 0029688736 scopus 로고    scopus 로고
    • Synthesis of pure tetramethylammonium peroxynitrite
    • Bohle, D. S., Glassbrenner, P. A., and Hansert, B. (1996) Synthesis of pure tetramethylammonium peroxynitrite, Methods Enzymol. 269, 302-311.
    • (1996) Methods Enzymol. , vol.269 , pp. 302-311
    • Bohle, D.S.1    Glassbrenner, P.A.2    Hansert, B.3
  • 20
    • 12644318998 scopus 로고
    • The first ionization of carbonic acid in aqueous solutions of sodium chloride
    • Harned, H. S., and Bonner, F. T. (1945) The first ionization of carbonic acid in aqueous solutions of sodium chloride, J. Am. Chem. Soc. 67, 1026-1031.
    • (1945) J. Am. Chem. Soc. , vol.67 , pp. 1026-1031
    • Harned, H.S.1    Bonner, F.T.2
  • 22
    • 0037470250 scopus 로고    scopus 로고
    • Reactions of deoxy-, oxy-, and methemoglobin with nitrogen monoxide. Mechanistic studies of the S-nitrosothiol formation under different mixing conditions
    • Herold, S., and Röck, G. (2003) Reactions of deoxy-, oxy-, and methemoglobin with nitrogen monoxide. Mechanistic studies of the S-nitrosothiol formation under different mixing conditions, J. Biol. Chem. 278, 6623-6634.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6623-6634
    • Herold, S.1    Röck, G.2
  • 23
    • 0014060675 scopus 로고
    • Determination of sulfhydryl groups with 2,2́- or 4,4́-dithiodipyridine
    • Grassetti, D. R., and Murray, J. F., Jr. (1967) Determination of sulfhydryl groups with 2,2́- or 4,4́-dithiodipyridine, Arch. Biochem. Biophys. 119, 41-49.
    • (1967) Arch. Biochem. Biophys. , vol.119 , pp. 41-49
    • Grassetti, D.R.1    Murray Jr., J.F.2
  • 24
    • 0033572288 scopus 로고    scopus 로고
    • Mechanistic studies of the oxidation of pyridoxalated hemoglobin polyoxyethylene conjugate (PHP) by nitrogen monoxide
    • Herold, S. (1999) Mechanistic studies of the oxidation of pyridoxalated hemoglobin polyoxyethylene conjugate (PHP) by nitrogen monoxide, Arch. Biochem. Biophys. 372, 393-398.
    • (1999) Arch. Biochem. Biophys. , vol.372 , pp. 393-398
    • Herold, S.1
  • 25
    • 0344844492 scopus 로고    scopus 로고
    • Metmyoglobin and methemoglobin catalyze the isomerization of peroxynitrite to nitrate
    • Herold, S., and Shivashankar, K. (2003) Metmyoglobin and methemoglobin catalyze the isomerization of peroxynitrite to nitrate, Biochemistry 42, 14036-14046.
    • (2003) Biochemistry , vol.42 , pp. 14036-14046
    • Herold, S.1    Shivashankar, K.2
  • 27
    • 0015239532 scopus 로고
    • Sulfheme proteins I. Optical and magnetic properties of sulfmyoglobin and its derivatives
    • Berzofsky, J. A., Peisach, J., and Blumberg, W. E. (1971) Sulfheme proteins I. Optical and magnetic properties of sulfmyoglobin and its derivatives, J. Biol. Chem. 246, 3367-3377.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3367-3377
    • Berzofsky, J.A.1    Peisach, J.2    Blumberg, W.E.3
  • 29
    • 0032928174 scopus 로고    scopus 로고
    • Direct observation of intermediates in the reaction of peroxynitrite with carbon dioxide
    • Meli, R., Nauser, T., and Koppenol, W. H. (1999) Direct observation of intermediates in the reaction of peroxynitrite with carbon dioxide, Helv. Chim. Acta 82, 722-725.
    • (1999) Helv. Chim. Acta , vol.82 , pp. 722-725
    • Meli, R.1    Nauser, T.2    Koppenol, W.H.3
  • 31
    • 0035916922 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies of the NO'-mediated oxidation of oxymyoglobin and oxyhemoglobin
    • Herold, S., Exner, M., and Nauser, T. (2001) Kinetic and mechanistic studies of the NO'-mediated oxidation of oxymyoglobin and oxyhemoglobin, Biochemistry 40, 3385-3395.
    • (2001) Biochemistry , vol.40 , pp. 3385-3395
    • Herold, S.1    Exner, M.2    Nauser, T.3
  • 33
    • 0242666822 scopus 로고    scopus 로고
    • Reaction of human hemoglobin with peroxynitrite: Isomerization to nitrate and secondary formation of protein radicals
    • Romero, N., Radi, R., Linares, E., Augusto, O., Detweiler, C. D., Mason, R. P., and Denicola, A. (2003) Reaction of human hemoglobin with peroxynitrite: Isomerization to nitrate and secondary formation of protein radicals, J. Biol. Chem. 278, 44049-44057.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44049-44057
    • Romero, N.1    Radi, R.2    Linares, E.3    Augusto, O.4    Detweiler, C.D.5    Mason, R.P.6    Denicola, A.7
  • 34
    • 0037116514 scopus 로고    scopus 로고
    • Product distribution of peroxynitrite decay as a function of pH, temperature, and concentration
    • Kissner, R., and Koppenol, W. H. (2002) Product distribution of peroxynitrite decay as a function of pH, temperature, and concentration, J. Am. Chem. Soc. 124, 234-239.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 234-239
    • Kissner, R.1    Koppenol, W.H.2
  • 37
    • 0033601102 scopus 로고    scopus 로고
    • Cage-escape of geminate radical pairs can produce peroxynitrate from peroxynitrite under a wide variety of experimental conditions
    • Hodges, G. R., and Ingold, K. U. (1999) Cage-escape of geminate radical pairs can produce peroxynitrate from peroxynitrite under a wide variety of experimental conditions, J. Am. Chem. Soc. 121, 10695-10701.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10695-10701
    • Hodges, G.R.1    Ingold, K.U.2
  • 39
    • 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
  • 40
    • 0037430191 scopus 로고    scopus 로고
    • Generation of a peroxynitrato metal complex from nitrogen dioxide and coordinated superoxide
    • Pestovsky, O., and Bakac, A. (2003) Generation of a peroxynitrato metal complex from nitrogen dioxide and coordinated superoxide, Inorg. Chem. 42, 1744-1750.
    • (2003) Inorg. Chem. , vol.42 , pp. 1744-1750
    • Pestovsky, O.1    Bakac, A.2
  • 41
    • 0000546575 scopus 로고
    • 2): A novel synthesis and some chemical and spectroscopic properties
    • 2): a novel synthesis and some chemical and spectroscopic properties, Inorg. Chem. 34, 787-791.
    • (1995) Inorg. Chem. , vol.34 , pp. 787-791
    • Appelman, E.H.1    Gosztola, D.J.2
  • 42
    • 84961981080 scopus 로고    scopus 로고
    • Peroxynitrate and peroxynitrite. A complete basis set investigation of similarities and differences between these NOx species
    • Olson, J. S., Bartberger, M. D., and Houk, K. N. (2003) Peroxynitrate and peroxynitrite. A complete basis set investigation of similarities and differences between these NOx species, J. Am. Chem. Soc. 125, 3999-4006.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3999-4006
    • Olson, J.S.1    Bartberger, M.D.2    Houk, K.N.3
  • 45
    • 0025259891 scopus 로고
    • In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides
    • Maples, K. R., Kennedy, C. H., Jordan, S. J., and Mason, R. P. (1990) In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides, Arch. Biochem. Biophys. 277, 402-409.
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 402-409
    • Maples, K.R.1    Kennedy, C.H.2    Jordan, S.J.3    Mason, R.P.4
  • 46
    • 0029864259 scopus 로고    scopus 로고
    • An EPR investigation of human methemoglobin. Oxidation by hydrogen peroxide: Methods to quantify all paramagnetic species observed in the reaction
    • Svistunenko, D. A., Patel, R. P., and Wilson, M. T. (1996) An EPR investigation of human methemoglobin. Oxidation by hydrogen peroxide: methods to quantify all paramagnetic species observed in the reaction, Free Rad. Res. 24, 269-280.
    • (1996) Free Rad. Res. , vol.24 , pp. 269-280
    • Svistunenko, D.A.1    Patel, R.P.2    Wilson, M.T.3
  • 47
    • 0027366718 scopus 로고
    • Detection and reactions of the globin radical in hemoglobin
    • McArthur, K. M., and Davies, M. J. (1993) Detection and reactions of the globin radical in hemoglobin, Biochim. Biophys. Acta 1202, 173-181.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 173-181
    • McArthur, K.M.1    Davies, M.J.2
  • 48
    • 0034612336 scopus 로고    scopus 로고
    • Scavenging of peroxynitrite by oxyhemoglobin and identification of modified globin residues
    • Minetti, M., Pietraforte, D., Carbone, V., Salzano, A. M., Scorza, G., and 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
  • 49
    • 3142775591 scopus 로고    scopus 로고
    • Pulse radiolysis studies of the reactions of carbonate radical anion with myoglobin and hemoglobin
    • Boccini, F., Domazou, A., and Herold, S. (2004) Pulse radiolysis studies of the reactions of carbonate radical anion with myoglobin and hemoglobin, J. Phys. Chem. A. 108, 5800-5805.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 5800-5805
    • Boccini, F.1    Domazou, A.2    Herold, S.3
  • 50
    • 0000695873 scopus 로고
    • Reactivity of the carbonate radical in aqueous solution. Tryptophan and its derivatives
    • Chen, S., and Huffman, M. Z. (1974) Reactivity of the carbonate radical in aqueous solution. Tryptophan and its derivatives, J. Phys. Chem. 78, 2099-202102.
    • (1974) J. Phys. Chem. , vol.78 , pp. 2099-202102
    • Chen, S.1    Huffman, M.Z.2
  • 51
  • 53
    • 0031853741 scopus 로고    scopus 로고
    • Peroxynitrite uncloaked?
    • Koppenol, W. H. (1998) Peroxynitrite uncloaked? Chem. Res. Toxicol. 11, 716-717.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 716-717
    • Koppenol, W.H.1
  • 54
    • 0142072014 scopus 로고    scopus 로고
    • Rate of ON-OO-bond homolysis and the Gibbs energy of formation of peroxynitrite
    • Lymar, S. V., and Poskrebyshev, G. A. (2003) Rate of ON-OO-bond homolysis and the Gibbs energy of formation of peroxynitrite, J. Phys. Chem. A. 107, 7991-7996.
    • (2003) J. Phys. Chem. A , vol.107 , pp. 7991-7996
    • Lymar, S.V.1    Poskrebyshev, G.A.2
  • 55
    • 0037069395 scopus 로고    scopus 로고
    • Myoglobin scavenges peroxynitrite without being significantly nitrated
    • Herold, S., Shivashankar, K., and Mehl, M. (2002) Myoglobin scavenges peroxynitrite without being significantly nitrated, Biochemistry 41, 13460-13472.
    • (2002) Biochemistry , vol.41 , pp. 13460-13472
    • Herold, S.1    Shivashankar, K.2    Mehl, M.3


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