80
Views
83
CrossRef citations to date
0
Altmetric
Original Article

Redox Cycling of Human Methaemoglobin by H2O2 Yields Persistent Ferryl Iron and Protein Based Radicals

, , , &
Pages 117-123 | Received 18 Dec 1995, Published online: 07 Jul 2009

References

  • Galaris D., Eddy L., Arduini A., Cadenas E., Hochstein P. Mechanism of reoxygenation injury in myocardial infarction: implications of a myoglobin redox cycle. Biochemical and Biophysical Research Communications 1989; 160: 1162–1168
  • Turner J. J.O., Rice-Evans C. A., Davies M. J., Newman E. S. Free radicals, myocytes and reperfusion injury. Biochemical Society Transactions 1990; 18: 1056–1059
  • Arduini A., Eddy L., Hochstein P. Detection of ferryl myoglobin in the isolated ischemic rat heart. Free Radical Biology and Medicine 1990; 9: 511–513
  • Cashon R. E., Alayash A. I. Reaction of human hemoglobin HbAo and two cross-linked derivatives with hydrogen peroxide: differential behavior of the ferryl intermediate. Archives of Biochemistry and Biophysics 1995; 316: 461–469
  • Alayash A. I., Fratantoni J. C., Bonaventura C., Bona-ventura J., Bucci E. Consequences of chemical modifications on the free radical reaction of human hemoglobin. Archives of Biochemistry and Biophysics 1992; 298: 114–120
  • George P., Irvine D. H. The reaction between metmyoglobin and hydrogen peroxide. The Biochemical Journal 1952; 52: 511–517
  • Kelso N., KingWinfield M. E. The mechanism of metmyoglobin oxidation. Journal of Biological Chemistry 1963; 238: 1520–1528
  • La G. N., Mar J., deRopp S., Latos-Grazynski L., Balch A. L., Johnson R. B., Smith K. M., Parish D. W., Cheng R. J. Proton NMR characterization of the ferryl group in model heme complexes and hemoproteins: evidence for the FeIVO group in ferryl myoglobin and Compound II of horseradish peroxidase. Journal of American Chemical Society 1983; 105: 782–787
  • Neuberger A., VanDeenen L. L.M., Rice-Evans C., Burden R. H. Free Radical Damage and its control. New Comprehensive Biochemistry Elsevier, Amsterdam 1994; vol. 28: 67–111
  • Giulivi C., Davies K. J.A. A novel antioxidant role for hemoglobin: a comproportionation of ferrylhemoglobin with oxyhemoglobin. The Journal of Biological Chemistry 1990; 265: 19453–19460
  • Yusa K., Shikama K. Oxidation of oxymyo-globin to metmyoglobin with hydrogen peroxide: involvement of ferryl intermediate. Biochemistry 1987; 26: 6684–6688
  • Antonini E., Brunori M. Haemoglobin and myoglobin in their reactions with ligands. North Holland Publishing company, Amsterdam 1971
  • KingKelso N., Looney F. D., Winfield M. E. Amino acid free radicals in oxidised metmyoglobin. Biochimica et Biophysica Acta 1967; 133: 65–82
  • Miki H., Harada K., Yamazaki I., Tamura M., Watanabe H. Electron spin resonance spectrum of Tyr-151 free radical formed in reaction of sperm whale metmyoglobin with ethyl hydroperoxide and potassium irridate. Archives of Biochemistry and Biophysics 1989; 275: 354–362
  • Davies M. J. Identification of a globin free radical in equine myoglobin treated with peroxides. Biochimica et Biophysica Acta 1991; 1077: 86–90
  • Cooper C. E., Green E. S.R., Rice-Evans C. A., Davies M. J., Wrigglesworth J. M. A hydrogen-donating monohydroxamate scavenges ferryl myoglobin radicals. Free Radical Research Communications 1994; 20: 219–227
  • Kelman D. L., Mason R. P. The myoglobin-derived radical formed on reaction of metmyoglobin with hydrogen peroxide is not a tyrosine peroxyl radical. Free Radical Research Communications 1992; 16: 27–33
  • Kelman D. J., De Gray J.A., Mason R. P. Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates. Journal of Biological Chemistry 1994; 269: 7458–7463
  • McArthur K. M., Davies M. J. Detection and reactions of the globin radical in haemoglobin. Biochimica et Biophysica Acta 1993; 1202: 173–181
  • Sard P., Hogg N., Darley-Usmar V. M., Sanna M. T., Wilson M. T. The oxidation of cytochrome-c oxidase vesicles by hemoglobin. Biochimica et Biophysica Acta 1994; 1208: 38–44
  • Yoshida Y., Kashiba K., Niki E. Free radical-mediated oxidation of lipids induced by hemoglobin in aqueous dispersions. Biochimica et Biophysica Acta 1994; 1201: 165–172
  • Rice C.-Evans. Oxidized low density lipoproteins. Free Radicals. From Basic Science to Medicine, G. Poli, E. Albano, M. U. Dianzini. Birkhausen, Basel 1993; 323–339
  • Hogg N., Rice C.-Evans, Darley-Usmar V., Wilson M. T., Paganga G., Bourne L. The role of lipid hydroperoxides in the myoglobin-dependent oxidation of LDL. Archives of Biochemistry and Biophysics 1994; 313: 39–44
  • Galaris D., Mira D., Sevanian A., Cadenas E., Hochstein P. Co-oxidation of salicylate and cholesterol during the oxidation of metmyoglobin by H2O2. Archives of Biochemistry and Biophysics 1988; 262: 221–231
  • Ortiz P. R., de Montellano Catalano C. E. Epoxidation of styrene by hemoglobin and myoglobin. Journal of Biological Chemistry 1985; 260: 9265–9271
  • Rice R. H., Lee Y. M., Brown W. D. Interaction of hemeproteinswithhydrogen peroxide: proteincrosslinking and covalent binding of benzo[fl]pyrene and 17B- estradiol. Archives of Biochemistry and Biophysics 1983; 221: 417–427
  • Grisham M. B. Myoglobinotalyzed hydrogen peroxide dependent arachidonic acid peroxidation. Journal of Free Radicals in Biology and Medicine 1985; 1: 227–232
  • Kelder P. P., de Mol N. J., Janssen L. H.M. Is hemoglobin a catalyst for sulfoxidation of chlorproma-zine? An investigation with isolated purified hemoglobin and hemoglobin in monooxygenase and peroxidase mimicking systems. Biochemical Pharmacology 1989; 38: 3593–3599
  • Kelder P. P., Fischer M. J.E., deMol N. J., Janssen L. H.M. Oxidation of chlorpromazine by methemoglobin in the presence of hydrogen peroxide. Formation of chlor-promazine radical cation and its covalent binding to methemoglobin. Archives of Biochemistry and Biophysics 1991; 284: 313–319
  • Bonaventura J., Schroeder W. A., Suen Fang. Human erythrocyte catalase: an improved method of isolation and a reevaluation of reported properties. Archives of Biochemistry and Biophysics 1972; 150: 606–617
  • Puppo A., Halliwell B. Formation of hydroxyl radicals from hydrogen peroxide in the presences of iron. Biochemical journal 1988; 249: 185–190
  • Gibson J. F., Ingram D. J.E. Location of free electrons in porphin ring complexes. Nature (London) 1956; 178(4538)871–872
  • Shiga T., Imaizumi K. Electron spin resonance study on peroxidase- and oxidase-reactions of horse radish peroxidase and methemoglobin. Archives of Biochemistry and Biophysics 1975; 167: 469–479
  • Tomoda A., Sugimoto K., Suhara M., Takeshita M., Yoneyama Y. Haemichrome formation from haemoglobin subunits by hydrogen peroxide. Biochemical Journal 1978; 171: 329–335
  • Mehlhorn R. J., Swanson C. E. Nitoxide-stimulated H2O2 decomposition by peroxidases and pseudoperoxidases. Free Radical Research Communications 1992; 17: 157–175
  • Mordente A., Martorana G. E., Santini S. A., Miggiano G. A.D., Petitti T., Giardina B., Battino M., Littarru G. P. Antioxidant effect of coenzyme Q on hydrogen peroxide-activated myoglobin. Clinical Investigator 1993; 71: S92–S96
  • Romero F. J., Ordoñez I., Arduini A., Cadenas E. The reactivity of thiols and disulfides with different redox states of myoglobin. Redox and addition reactions and formation of thiyl radical intermediates. Journal of Biological Chemistry 1992; 267: 1680–1688

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.