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Peroxynitrite Reacts with Methemoglobin to Generate Globin-Bound Free Radical Species

Implications for Vascular Injury
  • Chris E. Cooper
  • Jaume Torres
  • Martyn A. Sharpe
  • Mike T. Wilson
  • Dimitri A. Svistunenko
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 454)

Abstract

Reactive oxygen species been implicated in oxidative stress and vascular injury. These include the free radicals Superoxide (O2⋅)’ hydroxyl (OH⋅), peroxyl (LO2⋅) and alkoxyl (LO⋅) and the non-radicals hydrogen peroxide (H2O2), lipid peroxides and singlet oxygen. It was originally thought that the hydroxyl radical (OH⋅) was likely to be the most damaging species (1); however, this free radical is so reactive that it has a diffusion distance of no more than a few nm at most (2). The hydroxyl radical’s non-specific reactivity also makes it less likely that it will react with a vital cellular component. Other less reactive free radicals may be more toxic in that they can mediate damage at some distance from where they are formed.

Keywords

Nitric Oxide Free Radical Species Free Radical Superoxide Normal Human Blood Sperm Whale Myoglobin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Halliwell B, Gutteridge JMC. Oxygen free-radicals and iron in relation to biology and medicine—some problems and concepts. Arch. Biochem. Biophys. 1986; 246:501–514.PubMedCrossRefGoogle Scholar
  2. 2.
    Hutchinson F. The distance that a radical formed by ionizing radiation can diffuse in a yeast cell. Radiat. Res. 1957; 7:473–483.PubMedCrossRefGoogle Scholar
  3. 3.
    Darley-Usmar V, Wiseman H, Halliwell B. Nitric oxide and oxygen radicals: a question of balance. FEBS Lett. 1995; 369:131–135.PubMedCrossRefGoogle Scholar
  4. 4.
    Beckman JS. The physiological and pathological chemistry of nitric oxide. In: Lancaster J jr., ed. Nitric oxide: principals and actions. San Diego: Academic Press, 1996:1–82.CrossRefGoogle Scholar
  5. 5.
    Beckman JS, Ye YZ, Anderson PG, et al. Extensive nitration of protein tyrosines in human atherosclerosis detected by immunohistochemistry. Biol. Chem. Hoppe. Seylers 1994; 375:81–88.CrossRefGoogle Scholar
  6. 6.
    Kooy NW, Royall JA, Ye YZ, Kelly DR, Beckman JS. Evidence for in vivo peroxynitrite production in human acute lung injury. Amer. J. Resp. Crit. Care Med. 1995; 151:1250–1254.Google Scholar
  7. 7.
    Hantraye P, Brouillet E, Ferrante R, et al. Inhibition of neuronal nitric oxide synthase prevents MPTP-induced parkinsonism in baboons. Nature Medicine 1996; 2:1017–1021.PubMedCrossRefGoogle Scholar
  8. 8.
    Turrens JF, Boveris A. Generation of Superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 1980; 191:421–427.PubMedCentralPubMedGoogle Scholar
  9. 9.
    Brown GC, Cooper CE. Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal cytochrome oxidase respiration by competing with oxygen at cytochrome oxidase. FEBS Lett. 1994; 356:295–298.PubMedCrossRefGoogle Scholar
  10. 10.
    Cooper CE. Ferryl iron and protein free radicals. In: Rice-Evans CA, Burdon RH, eds. Free Radical Damage and its Control. Amsterdam: Elsevier, 1994:65–109.Google Scholar
  11. 11.
    Gibson JF, Ingram DJE. Location of free electrons in porphin ring complexes. Nature 1956; 178:871–872.CrossRefGoogle Scholar
  12. 12.
    Newman ESR, Rice-Evans CA, Davies MJ. Identification of initiating agents in myoglobin-induced lipid peroxidation. Biochem. Biophys. Res. Comm. 1991; 179:1414–1419.PubMedCrossRefGoogle Scholar
  13. 13.
    Kanner J, Harrel S. Initiation of membrane lipid peroxidation by activated metmyoglobin and methaemoglobin. Arch. Biochem. Biophys. 1975; 237:314–321.CrossRefGoogle Scholar
  14. 14.
    Giulivi C, Hochstein P, Davies KJA. Hydrogen peroxide production by red blood cells. Free Radical Biol. Med. 1994; 16:123–129.CrossRefGoogle Scholar
  15. 15.
    Svistunenko DA, Patel RP, Voloshchenko SV, Wilson MT. The globin-based free radical of ferryl hemoglobin is detected in normal human blood. J. Biol. Chem. 1997; 272:7114–7121.PubMedCrossRefGoogle Scholar
  16. 16.
    Patel RP, Svistunenko DA, Darley-Usmar VM, Symons MCR, Wilson MT. Redox cycling of human metHb by H2O2 yields persistent ferryl ion and protein based radicals: effect of catalase. Free Radical Res. 1996; 25:117–123.CrossRefGoogle Scholar
  17. 17.
    Uppu RM, Pryor WA. Biphasic synthesis of high concentrations of peroxynitrite using water-insoluble alkyl nitrite and hydrogen peroxide. Met. Enzymol. 1996; 269:322–329.CrossRefGoogle Scholar
  18. 18.
    Gorbunov NV, Osipov AN, Day BW, Zayas-Rivera B, Kagan VE, Elsayed NM. Reduction of Ferrylmyoglobin and Ferrylhemoglobin by Nitric Oxide: A Protective Mechanism against Ferryl Hemoprotein-Induced Oxidations. Biochemistry 1995; 34:6689–6699.PubMedCrossRefGoogle Scholar
  19. 19.
    Patel RP. Measurement of haemoglobin or copper ion promoted lipid peroxidation: implications for the oxidative modification of low density lipoprotein [PhD]: University of Essex, UK, 1996.Google Scholar
  20. 20.
    Svistunenko DA, Patel RP, Wilson MT. An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: methods to quantify all paramagnetic’ species observed in the reaction. Free Rad. Res. 1996; 24:269–280.CrossRefGoogle Scholar
  21. 21.
    Nicholls P. The formation and properties of sulphmyoglobin and sulphcatalase. Biochem. J. 1961; 81:374–383.PubMedCentralPubMedGoogle Scholar
  22. 22.
    Davies MJ. Detection of Metmyoglobin-Derived Radicals on Reaction of Metmyoglobin with Hydrogen Peroxide and Other Peroxidic Compounds. Free Rad. Res. Commun. 1990; 10:361–370.CrossRefGoogle Scholar
  23. 23.
    Petersen RL, Symons MCR, Taiwo FA. Application of Radiation and Electron Spin Resonance Spectroscopy to the Study of Ferryl Myoglobin. J. Chem. Soc. Faraday. Trans. 1 1989; 85:2435–2443.CrossRefGoogle Scholar
  24. 24.
    Tew D, deMontellano PO. The Myoglobin Protein Radical. Coupling of Tyr-103 to Tyr-151 in the H2O2-mediated cross-linking of sperm whale myoglobin. J. Biol. Chem. 1988; 263:17880–17886.PubMedGoogle Scholar
  25. 25.
    Gibson JF, Ingram DJE, Nicholls P. Free Radical produced in the Reaction of Metmyoglobin with Hydrogen Peroxide. Nature 1958; 181:1398–1399.PubMedCrossRefGoogle Scholar
  26. 26.
    DeGray JA, Gunther MR, TschirretGuth R, de Montellano PRO, Mason RP. Peroxidation of a specific tryptophan of metmyoglobin by hydrogen peroxide. J. Biol. Chem. 1997; 272(4):2359–2362.PubMedCrossRefGoogle Scholar
  27. 27.
    Svistunenko DA, Davies NA, Wilson MT, Stidwill RP, Singer M, Cooper CE. Free radical in blood: a measure of haemoglobin autoxidation in vivo? J. Chem. Soc. Perkin Trans. II 1997;In press.Google Scholar
  28. 28.
    Tan WKM, Williams CE, During MJ, et al. Accumulation of cytotoxins during the development of seizures and edema after hypoxic-ischemic injury In late-gestation fetal sheep. Pediatr. Res. 1996; 39(5):791–797.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Chris E. Cooper
    • 1
  • Jaume Torres
    • 1
  • Martyn A. Sharpe
    • 1
  • Mike T. Wilson
    • 1
  • Dimitri A. Svistunenko
    • 1
  1. 1.Department of Biological and Chemical Sciences Central CampusUniversity of EssexColchesterUK

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