Immunochemical detection of hemoglobin-derived radicals formed by reaction with hydrogen peroxide: Involvement of a protein-tyrosyl radical

Free Radical Biology and Medicine

Volumn 34, Issue 7, 2003, Pages 830-839

  Ramirez, Dario C ^a   Chen, Yeong Renn ^a   Mason, Ronald P ^a  

^a NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES   (United States)

Author keywords

Free radicals; Hemoglobin; Hydrogen peroxide; Immuno spin trapping; Red blood cells

Indexed keywords

5,5 DIMETHYL 1 PYRROLINE 1 OXIDE; ANTISERUM; ASCORBIC ACID; CYSTEINE; GLUTATHIONE; HEME; HEMOGLOBIN; HYDROGEN PEROXIDE; NITRONE; RADICAL; TYROSINE;

ANTIGEN BINDING; ARTICLE; CONTROLLED STUDY; DOSE RESPONSE; DRUG EFFECT; ELECTRON SPIN RESONANCE; ENZYME LINKED IMMUNOSORBENT ASSAY; ERYTHROCYTE; HUMAN; HUMAN CELL; IMMUNOCHEMISTRY; IODINATION; MALE; NORMAL HUMAN; OXIDATION; PRIORITY JOURNAL; REPRODUCIBILITY; SPIN TRAPPING; WESTERN BLOTTING;

ORYCTOLAGUS CUNICULUS;

EID: 0037376763     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(02)01437-5     Document Type: Article

References (49)

1. Frey P.A. Radical mechanisms of enzymatic catalysis. Annu. Rev. Biochem. 70:2001;121-148.
2. Alayash A.I., Patel R.P., Cashon R.E. Redox reactions of hemoglobin and myoglobin biological and toxicological implications . Antioxid. Redox Signal. 3:2001;313-327.
3. Ostdal H., Andersen H.J., Davies M.J. Formation of long-lived radicals on proteins by radical transfer from heme enzymes a common process . Arch. Biochem. Biophys. 362:1999;105-112.
4. Giulivi C., Cadenas E. Heme protein radicals formation, fate, and biological consequences . Free Radic. Biol. Med. 24:1998;269-279.
5. Svistunenko D.A. An EPR study of the peroxyl radicals induced by hydrogen peroxide in the heam proteins. Biochim. Biophys. Acta. 1546:2001;365-378.
6. DeGray J.A., Lassmann G., Curtis J.F., Kennedy T.A., Marnett L.J., Eling T.E., Mason R.P. Spectral analysis of the protein-derived tyrosyl radicals from prostaglandin H synthase. J. Biol. Chem. 267:1992;23583-23588.
7. 2. J. Biol. Chem. 274:1999;3308-3314.
8. 191 as the free radical site in cytochrome c peroxidase compound ES. Science. 245:1989;738-740.
9. Barr D.P., Gunther M.R., Deterding L.J., Tomer K.B., Mason R.P. ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide. J. Biol. Chem. 271:1996;15498-15503.
10. Gunther M.R., Sturgeon B.E., Mason R.P. A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide. Free Radic. Biol. Med. 28:2000;709-719.
11. Kelman D.J., Mason R.P. The myoglobin-derived radical formed on reaction of metmyoglobin with hydrogen peroxide is not a tyrosine peroxyl radical. Free Radic. Res. Commun. 16:1992;27-33.
12. Maples K.R., Jordan S.J., Mason R.P. In vivo rat hemoglobin thiyl free radical formation following administration of phenylhydrazine and hydrazine-based drugs. Drug Metab. Dispos. 16:1988;799-803.
13. Maples K.R., Kennedy C.H., Jordan S.J., Mason R.P. In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides. Arch. Biochem. Biophys. 277:1990;402-409.
14. McArthur K.M., Davies M.J. Detection and reactions of the globin radical in haemoglobin. Biochim. Biophys. Acta. 1202:1993;173-181.
15. 2 and a ferryl species. Biochemistry. 38:1999;2078-2087.
16. Alayash A.I. Hemoglobin-based blood substitutes oxygen carriers, pressor agents, or oxidants . Nat. Biotechnol. 17:1999;545-549.
17. Everse J., Hsia N. The toxicities of native and modified hemoglobins. Free Radic. Biol. Med. 22:1997;1075-1099.
18. Irwin J.A., Ostdal H., Davies M.J. Myoglobin-induced oxidative damage evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants . Arch. Biochem. Biophys. 362:1999;94-104.
19. Kelman D.J., DeGray J., Mason R.P. Reaction of myoglobin with hydrogen peroxide forms peroxyl radical which oxidizes substrates. J. Biol. Chem. 269:1994;7458-7463.
20. Giulivi C., Cadenas E. Ferrylmyoglobin formation and chemical reactivity toward electron-donating compounds . Methods Enzymol. 233:1994;189-202.
21. Shiga T., Imaizumi K. Electron spin resonance study on peroxidase- and oxidase-reactions of horse radish peroxidase and methemoglobin. Arch. Biochem. Biophys. 167:1975;469-479.
22. 2 yields persistent ferryl iron and protein based radicals. Free Radic. Res. 25:1996;117-123.
23. Giulivi C., Davies K.J.A. Hydrogen peroxide-mediated ferrylhemoglobin generation in vitro and in red blood cells. Methods Enzymol. 231:1994;490-496.
24. Svistunenko D.A., Patel R.P., Voloshchenko S.V., Wilson M.T. The globin-based free radical of ferryl hemoglobin is detected in normal human blood. J. Biol. Chem. 272:1997;7114-7121.
25. Davies M.J., Gilbert B.C., Haywood R.M. Radical-induced damage to proteins E.S.R. spin-trapping studies . Free Radic. Res. Commun. 15:1991;111-127.
26. Mason R.P. In vivo spin trapping. Rhodes C.J. Toxicology of the human environment. 2000;49-70 Taylor & Francis, Liverpool, England.
27. Gunther M.R., Tschirret-Guth R.A., Witkowska H.E., Fann Y.C., Barr D.P., Ortiz De Montellano P.R., Mason R.P. Site-specific spin trapping of tyrosine radicals in the oxidation of metmyoglobin by hydrogen peroxide. Biochem. J. 330:1998;1293-1299.
28. 2. Involvement of a thiyl radical produced at cysteine 110. J. Biol. Chem. 275:2000;20391-20398.
29. 2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical. J. Biol. Chem. 276:2001;16540-16547.
30. Detweiler C.D., Deterding L.J., Tomer K.B., Chignell C.F., Germolec D., Mason R.P. Immunological identification of the heart myoglobin radical formed by hydrogen peroxide. Free Radic. Biol. Med. 33:2002;364-369.
31. •OOH. Free Radic. Res. Commun. 10:1990;11-15.
32. Winterbourn C.C. Oxidative reactions of hemoglobin. Methods Enzymol. 186:1990;265-272.
33. Faivre B., Menu P., Labrude P., Vigneron C. Hemoglobin autooxidation/oxidation mechanisms and methemoglobin prevention or reduction processes in the bloodstream. Literature review and outline of autooxidation reaction. Art. Cells Blood Subs. Immob. Biotech. 26:1998;17-26.
34. Yoo Y.-M., Kim K.-M., Kim S.-S., Han J.-A., Lea H.-Z., Kim Y.-M. Hemoglobin toxicity in experimental bacterial peritonitis is due to production of reactive oxygen species. Clin. Diagn. Lab. Immunol. 6:1999;938-945.
35. Grisham M.B., Gaginella T.S., von Ritter C., Tamai H., Be R.M., Granger D.N. Effects of neutrophil-derived oxidants on intestinal permeability, electrolyte transport, and epithelial cell viability. Inflammation. 14:1990;531-542.
36. Misra H.P., Fridovich I. The generation of superoxide radical during the autoxidation of hemoglobin. J. Biol. Chem. 247:1972;6960-6962.
37. Giulivi C., Hochstein P., Davies K.J.A. Hydrogen peroxide production by red blood cells. Free Radic. Biol. Med. 16:1994;123-129.
38. Iuliano L., Violi F., Pedersen J.Z., Pratico D., Rotilio G., Balsano F. Free radical-mediated platelet activation by hemoglobin released from red blood cells. Arch. Biochem. Biophys. 299:1992;220-224.
39. Kindt J.T., Woods A., Martin B.M., Cotter R.J., Osawa Y. Covalent alteration of the prosthetic heme of human hemoglobin by BrCCl3. Cross-linking of heme to cysteine residue 93. J. Biol. Chem. 267:1992;8739-8743.
40. Kim Y.-M., Jeong S.-H., Yamazaki I., Piette L.H., Han S., Hong S.-J. Decay studies of DMPO-spin adducts of free radicals produced by reactions of metmyoglobin and methemoglobin with hydrogen peroxide. Free Radic. Res. 22:1995;11-21.
41. Nagababu E., Ramasamy S., Rifkind J.M., Jia Y., Alayash A.I. Site-specific cross-linking of human and bovine hemoglobins differentially alters oxygen binding and redox side reactions producing rhombic heme and heme degradation. Biochemistry. 41:2002;7407-7415.
42. Mao G.D., Thomas P.D., Poznansky M.J. Oxidation of spin trap 5,5-dimethyl-1-pyrroline-1-oxide in an electron paramagnetic resonance study of the reaction of methemoglobin with hydrogen peroxide. Free Radic. Biol. Med. 16:1994;493-500.
43. McIntire G.L., Blount H.N., Stronks H.J., Shetty R.V., Janzen E.G. Spin trapping in electrochemistry. 2. Aqueous and nonaqueous electrochemical characterizations of spin traps. J. Phys. Chem. 84:1980;916-921.
44. George P., Irvine D.H. A possible structure for the higher oxidation state of metmyoglobin. Biochem. J. 60:1955;596-604.
45. Yamazaki I., Tamura M., Nakajima R. Horseradish peroxidase C. Mol. Cell. Biochem. 40:1981;143-153.
46. 2+). J. Phys. Chem. 88:1984;99-101.
47. Sturgeon B.E., Sipe H.J. Jr., Barr D.P., Corbett J.T., Martinez J.G., Mason R.P. The fate of the oxidizing tyrosyl radical in the presence of glutathione and ascorbate. Implications for the radical sink hypothesis. J. Biol. Chem. 273:1998;30116-30121.
48. 2-activated metmyoglobin and other proteins. Free. Radic. Biol. Med. 23:1997;754-761.
49. Hawkins C.L., Davies M.J. Generation and propagation of radical reactions on proteins. Biochim. Biophys. Acta. 1504:2001;196-219.