Photodynamically generated bovine serum albumin radicals: Evidence for damage transfer and oxidation at cysteine and tryptophan residues

Free Radical Biology and Medicine

Volumn 24, Issue 5, 1998, Pages 754-766

  Silvester, Julie A ^a   Timmins, Graham S ^a   Davies, Michael J ^b  

^a UNIVERSITY OF YORK   (United Kingdom)

^b HEART RESEARCH INSTITUTE   (Australia)

Author keywords

EPR; Free radical; Photooxidation; Protein oxidation; Radicals; Spin trapping; Thiyl radicals; Tryptophan radicals

Indexed keywords

BOVINE SERUM ALBUMIN; CYSTEINE; FREE RADICAL; HEMATOPORPHYRIN; PORPHYRIN; TETRAMETHYLENEPYRIDINIUM PORPHYRIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; BLEACHING; CONTROLLED STUDY; DIALYSIS; ELECTRON SPIN RESONANCE; FLUORESCENCE SPECTROSCOPY; NONHUMAN; PH; PHOTOLYSIS; PHOTOOXIDATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN STRUCTURE;

BICYCLO COMPOUNDS, HETEROCYCLIC; CYSTEINE; FREE RADICALS; HEMATOPORPHYRINS; HYDROGEN-ION CONCENTRATION; OXIDATION-REDUCTION; PHOSPHITES; PHOTIC STIMULATION; PHOTOSENSITIZING AGENTS; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE; SPIN TRAPPING; TRYPTOPHAN;

BOVINAE;

EID: 0032520869     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(97)00327-4     Document Type: Article

References (48)

1. Halliwell B., Gutteridge J. M. C. Free radicals in biology and medicine. 2nd edn. 1989;Clarendon Press, Oxford.
2. Davies M. J., Dean R. T. Radical-mediated protein oxidation From chemistry to medicine . 1997;Oxford University Press, Oxford.
3. Dean R. T., Fu S., Stocker R., Davies M. J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324:1997;1-18.
4. Wolff S. P., Garner A. W., Dean R. T. Free radicals, lipids and protein degradation. Trends Biochem. Sci. 11:1986;27-31.
5. Stadtman E. R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalysed reactions. Ann. Rev. Biochem. 62:1993;797-821.
6. Pacifici R. E., Davies K. J. A. Protein, lipid and DNA repair systems in oxidative stress The free radical theory of aging revisited . Gerontology. 37:1991;166-180.
7. Garrison W. M. Reaction mechanisms in the radiolysis of peptides, polypeptides and proteins. Chem. Rev. 87:1987;381-398.
8. Simpson J. A., Narita S., Gieseg S., Gebicki S., Gebicki J. M., Dean R. T. Long-lived reactive species on free-radical-damaged proteins. Biochem. J. 282:1992;621-624.
9. Davies K. J. A. Protein damage and degradation by oxygen radicals. 1. General aspects. J. Biol. Chem. 267:1987;9895-9901.
10. Cabiscol E., Levine R. L. Carbonic anhydrase III. Oxidative modification in vivo and loss of phosphatase activity during aging. J. Biol. Chem. 270:1995;14742-14747.
11. Davies M. J., Fu S., Dean R. T. Protein hydroperoxides can give rise to reactive free radicals. Biochem. J. 305:1995;643-649.
12. Davies M. J. Protein and peptide alkoxyl radicals can give rise to C-terminal decarboxylation and backbone cleavage. Arch. Biochem. Biophys. 336:1996;163-172.
13. Butler, J.; Land, E. J.; Prutz, W. A.; Swallow, A. J. Charge transfer between tryptophan and tyrosine residues in peptides. Biochim. Biophys. Acta 705:250-162; 1982.
14. Prutz W. A., Butler J., Land E. J. Methionyl → tyrosyl radical transitions initiated by Br2-· in peptide model systems and ribonuclease A. Int. J. Radiat. Biol. 47:1985;149-156.
15. Faraggi W. A., Steiner J. P., Klapper M. H. Intramolecular electron and proton-transfer in proteins - CO2-· reduction of riboflavin binding-protein and ribonuclease A. Biochemistry. 24:1985;3273-3279.
16. Butler J., Land E. J., Prutz W. A., Swallow A. J. The role of sulfur peptide functions in free-radical transfer - A pulse-radiolysis study. Int. J. Radiat. Biol. 55:1989;539-556.
17. Bobrowski K., Wierzchowski K. L., Holcman J., Ciurak H. Intramolecular electron transfer in peptides containing methionine, tryptophan and tyrosine A pulse-radiolysis study . Int. J. Radiat. Biol. 57:1990;919-932.
18. Stadtman E. R. Metal ion-catalysed oxidation of proteins Biochemical mechanism and biological consequences . Free Radic. Biol. Med. 9:1990;315-325.
19. Levine R. L. Mixed-function oxidation of histidine residues. Wold F., Moldave K. Methods in enzymology. Vol. 107:1984;370-376 Academic Press, San Diego.
20. Levine R. L., Garland D., Oliver C. N., Amici A., Climent I., Lenz A.-G., Ahn B.-W., Shattiel S., Stadtman E. R. Determination of carbonyl content in oxidatively modified proteins. Packer L., Glazer A. N. Methods in enzymology. Vol. 186:1990;464-478 Academic Press, San Diego.
21. Davies M. J., Gilbert B. C., Haywood R. M. Radical-induced damage to proteins ESR spin trapping studies . Free Radic. Res. Commun. 15:1991;111-127.
22. Davies M. J., Gilbert B. C., Haywood R. M. Radical-induced damage to BSA Role of the cysteine residue . Free Radic. Res. Commun. 18:1993;353-367.
23. Davies M. J. Detection and identification of macromolecule-derived radicals by EPR spin trapping. Res. Chem. Intermed. 19:1993;669-679.
24. Timmins G. S., Davies M. J. An EPR spin trapping study of albumin protein radicals formed by the photodynamic action of haematoporphyrin. J. Photochem. Photobiol.: B. Biol. 21:1993;167-173.
25. Timmins G. S., Davies M. J. Conformational changes induced in bovine serum albumin by the photodynamic action of haematoporphyrin. J. Photochem. Photobiol.: B. Biol. 24:1994;117-122.
26. Cohen S., Margalit R. Binding of porphyrin to human serum albumin. Biochem. J. 270:1990;325-330.
27. Kaur, H.; Leung, K. H. W., Perkins, M. J. A water-soluble nitroso-aromatic spin trap. J. Chem. Soc. Chem. Commun. 142-143; 1981.
28. Peters T. Serum albumin. Anfinsen C. B., Edsall J. T., Richards F. M. Advances in protein chemistry. Vol. 37:1985;161-245 Academic Press, San Diego.
29. Teale F. W. J. The ultraviolet fluorescence of proteins in neutral solution. Biochem. J. 76:1960;381-388.
30. Rosenberger V., Margalit R. Thermodynamics of the binding of hematoporphyrin ester, a hematoporphyrin derivative-like sensitizer, and its components to human serum albumin, human high-density-lipoprotein and human low-density-lipoprotein. Photochem. Photobiol. 58:1993;627-630.
31. Wolff S. P., Dean R. T. Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymic hydrolysis. Biochem. J. 234:1986;399-403.
32. Silvester, J. A.; Davies, M. J.; Timmins, G. S. A study of photochemically-generated protein radical spin adducts on bovine serum albumin: Genuine spin-trapping and artifactual non-radical addition in the same molecule. Redox Report. In press; 1997.
33. Buettner G. R. Spin trapping ESR parameters of spin adducts . Free Radic. Biol. Med. 3:1987;259-303.
34. Carter D. C., Ho J. H. Structure of serum albumin. Anfinsen C. B., Edsall J. T., Richards F. M., Eisenberg D. S. Advances in protein chemistry. Vol. 45:1994;153-203 Academic Press, San Diego.
35. Wagner J. R., Ali H., Langlois R., Brasseur N., van Lier J. E. Biological activities of phthalocyanines. VI. Photo-oxidation of L-tryptophan by selectively sulphonated gallium phthalocyanines: Singlet oxygen yields and effects of aggregation. Photochem. Photobiol. 45:1987;587-594.
36. Spikes J. D. Quantum yields and kinetics of the photobleaching of hematoporphyrin, Photofrin-II, tetra (4-sulfonatophenyl)-porphine and uroporphyrin. Photochem. Photobiol. 55:1992;797-808.
37. Vergeldt F. J., Koehorst R. B. M., van Hoek A., Schaafsme T. J. Intramolecular interactions in the ground and excited state of tetrakis(N-methylpyridyl)[orphyrins. J. Phys. Chem. 99:1995;4397-4405.
38. Gunther M. R., Kelman D. J., Corbett J. T., Mason R. P. Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical. J. Biol. Chem. 270:1995;16075-16081.
39. 2-mediated cross-linking of sperm whale myoglobin. J. Biol. Chem. 263:1988;17880-17886.
40. Davies M. J. Identification of a globin free radical in equine myoglobin treated with peroxides. Biochim. Biophys. Acta. 1077:1988;86-90.
41. 2. J. Biol. Chem. 267:1992;8827-8833.
42. Rao S. I., Wilks A., Ortiz de Montellano P. R. The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and beta-methylstyrene by recombinant sperm whale myoglobin. J. Biol. Chem. 268:1993;803-809.
43. DeGray J. A., Gunther M. R., Tschirret-Guth R., Ortiz de Montellano P. R., Mason R. P. Peroxidation of a specific tryptophan of metmyoglobin by hydrogen peroxide. J. Biol. Chem. 272:1997;2359-2362.
44. 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.
45. McArthur K. M., Davies M. J. Detection and reactions of the globin radical in haemoglobin. Biochim. Biophys. Acta. 1202:1993;173-181.
46. Pedersen J. Z., Finazzi A. A. Protein-radical enzymes. FEBS Lett. 325:1993;53-58.
47. Rova U., Goodtzova K., Ingemarson R., Behravan G., Graslund A., Thelander L. Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase. Biochemistry. 34:1995;4267-4275.
48. Licht S., Gerfen G. J., Stubbe J. Thiyl radicals in ribonucleotide reductases. Science. 271:1996;477-481.