Oxidation of melatonin by oxoferryl hemoglobin: A mechanistic study

References

• Jovanovic S.V., Steenken S. Substituent effect on the spectral, acid base and redox properties of indolyl radicals: a pulse radiolysis study. Journal of Physical Chemistry 1992; 96: 6674–6679
   Web of Science ®Google Scholar
• Al-Kazwini A.T., O'Neill P., Adams G.E., Cundall R.B. One-electron oxidation of methoxylated and hydroxylated indoles by azide 1. Characterization of primary indolic radicals. Journal of Physical Chemistry 1990; 94: 6666–6670
   Web of Science ®Google Scholar
• Solar S., Getoff N., Surdhar P.S., Armstrong D. Oxidation of tryptophan and N-methylindole by N3, Br2/·-, (SNC)2/·- radicals in light and heavy water solutions. A pulse radiolysis study. Journal of Physical Chemistry 1991; 95: 3639–3643
   Web of Science ®Google Scholar
• Shen X., Lind J., Merenyi G. One-electron oxidation of indoles and acid base properties of the indolyl radicals. Journal of Physical. Chemistry 1987; 91: 4403–4406
   Web of Science ®Google Scholar
• Land E.J., Prütz W.A. Fast one-electron oxidation of tryptophan by azide radicals. International Journal of Radiation Biology 1969; 32: 203–207
   Google Scholar
• Redpath J.L., Santus R., Ovadia J., Grossweiner L.I. The oxidation of tryptophan by radical anions. International Journal of Radiation Biology 1975; 27: 201–204
   Web of Science ®Google Scholar
• Mahal H.S., Sharma H.S., Mukherjee T. Antioxidant properties of melatonin: a pulse radiolysis study. Free Radical Biology and Medicine 1999; 26: 557–565
   PubMed Web of Science ®Google Scholar
• Tan D.-X., Chen L.D., Poeggeler B., Manchester L.D., Reiter R.J. Melatonin: a potent, endogenous hydroxyl radical scavenger. Endocrine Journal 1993; 1: 57–60
   Google Scholar
• Scaiano J.C. Exploratory laser flash photolysis study of free radical reactions and magnetic field effects in melatonin chemistry. Journal of Pineal Research 1995; 19: 189–195
   PubMed Web of Science ®Google Scholar
• Pieri C., Marra M., Moroni F., Recchioni R., Marcheselli F. Melatonin: a peroxyl radical scavenger more effective than vitamin E. Life Sciences 1994; 55: 271–276
   Web of Science ®Google Scholar
• Livrea M.A., Tesoriere L., D'Arpa D., Morreale M. Reaction of melatonin with lipoperoxyl radicals in phospholipid bilayers. Free Radical Biology and Medicine 1997; 23: 706–711
   PubMed Web of Science ®Google Scholar
• Marshall K.-A., Reiter R.J., Poeggeler B., Aruoma O.I., Halliwell B. Evaluation of the antioxidant activity of melatonin in vitro. Free Radical Biology and Medicine 1996; 21: 307–315
   PubMed Web of Science ®Google Scholar
• Tan D.-X., Manchester L.C., Reiter R.J., Plummer B.F., Hardies L.J., Weintraub S.T., Vijayalaxmi S.T., Shepherd A.M.M. A novel melatonin metabolite, cyclic 3-hydroxymelatonin: a biomarker of in vivo hydroxyl radical generation. Biochemical and Biophysical Research Communications 1998; 253: 614–620
   PubMed Web of Science ®Google Scholar
• Zhang H., Squadrito G.L., Pryor W.A. The reaction of melatonin with peroxinitrite: formation of melatonin radical cation and absence of stable nitrated products. Biochemical and Biophysical Research Communications 1998; 251: 83–87
   PubMedGoogle Scholar
• Roberts J.E., Hu J.E., Wishart J.F. Pulse radiolysis study of melatonin and chloromelatonin. Journal of Photochemistry and Photobiology B—Biology 1998; 42: 125–132
   PubMed Web of Science ®Google Scholar
• Zhang H., Squadrito G.L., Uppu R., Pryor W.A. Reaction of peroxyxynitrite with melatonin: a mechanistic study. Chemical Research in Toxicology 1999; 12: 526–534
   PubMed Web of Science ®Google Scholar
• Poeggeler B., Saarela S., Reiter R.J., Tan D.-X., Chen L.-D., Manchester L.C., Barlow-Walden L.R. Melatonin. A highly potent endogenous scavenger and electron donor: new aspects of the oxidation chemistry of this indole accessed in vitro. Annals of the New York Academy of Sciences 1994; 738: 419–420
   PubMed Web of Science ®Google Scholar
• Stasica P.P., Ulanski P., Rosiak J.M. Reactions of melatonin with radicals in deoxygenated aqueous solution. Journal of Radioanalytical and Nuclear Chemistry 1998; 232: 107–113
   Web of Science ®Google Scholar
• Hardeland R., Reiter R.J., Poeggeler B., Tan D.-X. The significance of the metabolism of the neurohormone melatonin: antioxidative protection and formation of bioactive substances. Neuroscience and Biobehavioral Reviews 1993; 17: 347–357
   PubMed Web of Science ®Google Scholar
• Dellegar S.M., Murphy S.A., Bourne A.E., Di Cesare J.C., Purser G.H. Identification of the factors affecting the rate of deactivation of hypochlorous acid by melatonin. Biochemical and Biophysical Research Communications 1999; 257: 431–439
   PubMedGoogle Scholar
• Everse J., Hsia N. The toxicities of native and modified hemoglobins. Free Radical Biology and Medicine 1997; 22: 1075–1099
   PubMed Web of Science ®Google Scholar
• Halliwell B., Gutteridge J.M.C. Free Radicals in Biology and Medicine. Clarendon Press, Oxford 1999; 3
   Google Scholar
• Tesoriere L., Allegra M., D'Arpa D., Butera D., Livrea M.A. Reaction of melatonin with hemoglobin-derived oxoferryl radicals and inhibition of the hydroperoxide-induced hemoglobin denaturation in red blood cells. Journal of Pineal Research 2001
   PubMedGoogle Scholar
• Patel R.P., Svistunenko D.A., Darley-Usmar V.M., Symons M.C.R., Wilson M.T. Redox cycling of human methaemoglobin by H2O2 yields persistent ferryl iron and protein based radicals. Free Radical Research Communications 1996; 25: 117–123
   Google Scholar
• Winterbourn C.C. Oxidative reactions of hemoglobin. Methods in Enzymology, L. Packer, A.N. Glazer. Academic Press, San Diego, CA 1990; 186: 265–272, In
   Google Scholar
• Gringberg L.N., Rachmilewitz E.A., Newmark H. Protective effects of rutin against hemoglobin oxidation. Biochemical Pharmacology 1994; 48: 643–649
   PubMedGoogle Scholar
• Vitale A., Ferrari C., Aldana H., Affanni J. Highly sensitive method for the determination of melatonin by normal-phase high performance liquid chromatography with fluorimetric detection. Journal of Chromatography B 1996; 681: 381–384
   PubMedGoogle Scholar
• McArthur K.M., Davies M.J. Detection and reactions of the globin radical in haemoglobin. Biochimica et Biophysica Acta 1993; 1202: 173–181
   PubMed Web of Science ®Google Scholar
• Giulivi C., Cadenas E. Heme protein radicals: formation fate, and biological consequences. Free Radical Biology and Medicine 1998; 24: 269–279
   PubMed Web of Science ®Google Scholar
• Davies M.J. Detection of peroxyl and alkoxyl radicals produced by reaction of hydroperoxides with heme-proteins by electron spin resonance spectroscopy. Biochimica et Biophysica Acta 1988; 964: 28–35
   PubMed Web of Science ®Google Scholar
• Davies M.J. Identification of a globin free radical in equine myoglobin treated with peroxides. Biochimica et Biophysica Acta 1991; 1077: 86–90
   PubMed Web of Science ®Google Scholar
• Everse J. The structure of heme-proteins compounds I and II: some misconceptions. Free Radical Biology and Medicine 1998; 24: 1338–1346
   PubMed Web of Science ®Google Scholar
• Sugimoto H., Tung H.-C., Sawyer D.T. Formation, characterization and reactivity of the oxene adduct of [tetrakis(2,6-dichloro-phenyl)porphinato]iron(III) perchlorate in acetonitrile. Model for the reactive intermediate of cytochrome P-450. Journal of the American Chemical Society 1988; 110: 2465–2470
   Web of Science ®Google Scholar
• Giulivi C., Davies K.J.A. A novel antioxidant role for hemoglobin. Journal of Biological Chemistry 1990; 265: 19453–19460
   PubMed Web of Science ®Google Scholar
• Koppenol W.H., Liebman J.F. The oxidizing nature of the hydroxyl radical: a comparison with the ferryl ion (FeO2+). Journal of Physical Chemistry 1983; 88: 99–101
   Google Scholar
• Shiga T., Imaizumi K. Electron spin resonance study on peroxidase- and oxidase-reactions of horseradish peroxidase and methemoglobin. Archives of Biochemistry and Biophysics 1975; 167: 469–479
   PubMed Web of Science ®Google Scholar
• Kopin I.J., Pare C.M.B., Axelrod J., Werissbach H. The fate of melatonin in animals. Journal of Biological Chemistry 1961; 236: 3072–3075
   PubMed Web of Science ®Google Scholar
• Hirata F., Hayaishi O., Tokuyama T., Senoh S. In vitro and in vivo formation of two new metabolites of melatonin. Journal of Biological Chemistry 1974; 249: 1311–1313
   PubMed Web of Science ®Google Scholar
• Hardeland R., Fuhrberg B., Behrmann G., Balzer I. Sleep-latency reducing pineal hormone melatonin as a scavenger of free radicals: hemin-catalysed formation of N1-acetyl-N2-formyl-5-meth-oxykynuramine. Sleep Research 1993; 22: 621–628
   Google Scholar
• Tan D.-X., Manchester L.C., Reiter R.J., Plummer B.F., Limson J., Weintraub S.T., Qi W. Melatonin directly scavenges hydrogen peroxide: a potentially new metabolic pathway of melatonin biotransformation. Free Radical Biology and Medicine 2000; 29: 1177–1185
   PubMed Web of Science ®Google Scholar
• Nagababu E., Rifkind J.M. Reaction of hydroperoxide with ferryl hemoglobin: superoxide production and heme degradation. Biochemistry 2000; 39: 12503–12511
   PubMed Web of Science ®Google Scholar
• Dunford H.B. Heme peroxidases. Wiley and Sons, New York 1999
   Google Scholar