Micellar effect on tyrosine one-electron oxidation by azide radicals

Radiation Physics and Chemistry

Volumn 72, Issue 4, 2005, Pages 497-506

  Ionescu, A ^a,b   Grand, D ^a   Sicard Roselli, C ^a   Houee Levin C ^a  

^a UNIVERSITÉ PARIS SUD   (France)

^b HORIA HULUBEI NATIONAL INSTITUTE OF PHYSICS AND NUCLEAR ENGINEERING   (Romania)

Author keywords

Direct micelles; Dityrosine; Gamma and pulse radiolysis

Indexed keywords

FREE RADICALS; GAMMA RAYS; MICELLES; RADIOLYSIS; SOLUTIONS;

AZIDE RADICALS; INTERFACIAL CHARGE; ONE-ELECTRON OXIDATION; TYROSINE;

OXIDATION;

AZIDE;

AQUEOUS SOLUTION; ARTICLE; CHEMICAL REACTION; ELECTRON TRANSPORT; GAMMA RADIATION; MICELLE; MICELLIZATION; OXIDATION KINETICS; RADIOLYSIS; REACTION ANALYSIS; STEADY STATE;

EID: 9944253049     PISSN: 0969806X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.radphyschem.2003.10.015     Document Type: Article

References (36)

1. Alfassi Z.B., Schuler R.H. Reaction of azide radicals with aromatic compounds. Azide as a selective oxidant. J. Phys. Chem. 89:1985;3359-3363
2. Bayse G.S., Michaels A.W., Morrison M. The peroxidase catalyzed oxidation of tyrosine. Biochim. Biophys. Acta. 284:1972;34-42
3. Bensasson, R.V., Land, E.J., Truscott, T.G., 1993. Excited States and Free Radicals in Biology and Medicine. Oxford University press, Oxford, pp. 173-200.
4. Bernas, A., Grand, D., Hauteclocque, S., 1991. In: Excess Electrons in Dielectric Media. CRC Press, Boca Raton, pp. 367-396.
5. Berthod A. Structures physico-chimiques des milieux dispersés, micelles, emulsions et microémulsions. J. Chim. Phys. 80:1983;407-424
6. Burlakova E.B., Mikhailov V.F., Azurik V.K. The redox homeostasis system in radiation-induced genomic instability. Radiats biol. Radioecol. 41:2001;489-499
7. Cardoso da Silva R., Olofson G., Schillen K., Loh W. Influence of ionic surfactants on the aggregation of poly (ethylene oxide)-poly (propylene oxide)-poly (ethylene oxide) block copolymers studied by differential scanning and isothermal titration calorimetry. J. Phys. Chem. B. 106:2002;1239-1246
8. Cheng C.M., Hong H.J., Liu J.C., Shih N.L., Juan S.H., Loh S.H., Chan P., Chen J.J., Cheng T.H. Crucial role of extracellular signal-regulated kinase pathway in reactive oxygen species-mediated endothelin-1 gene expression induced by endothelin-1 in rat cardiac fibroblasts. Mol. Pharmacol. 63:2003;1002-1011
9. Chiarugi P., Pani G., Giannoni E., Taddei L., Colavitti R., Raugei G., Symons M., Borrello S., Galeotti T., Ramponi G. Reactive oxygen species as essential mediators of cell adhesion. the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion J. Cell Biol. 161:2003;933-944
10. Encinas M.V., Lissi E.A. Quenching of pyrene fluorescence by tryptophan in micellar solutions. Photochem. Photobiol. 44:1986;579-585
11. Favaudon, V., Tourbez, C., Houée-Levin, J.M., Lhoste, 1990. Carboxyl radical induced cleavage of disulfide bonds in proteins. A gamma-ray and pulse mechanistic investigation. Biochemistry. 29, 10978-10989.
12. Fendler, J.H., Fendler, E.J., 1975. Catalysis in Micellar and Macromolecular Systems. Academic Press, New York, pp. 105-120.
13. Funasaki N. Gel filtration chromatography study on the self-association os surfactants and related compounds. Adv.Colloid Interface Sci. 43:1993;87-136
14. Gill S.G., Von Hippel P.H. Calculations of protein extinction coefficients from amino-acid sequence data. Anal. Biochem. 182:1989;319-322
15. Giulivi C., Davies K.J. Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19. S) proteasome J. Biol. Chem. 268:1993;8752-8759
16. Hautecloque S., Grand D., Bernas A. Salt effects on photoionization yields in micellar systems. J. Phys. Chem. 89:1995;2705-2708
17. Houée-Levin C., Sicard-Roselli C. Radiation chemistry of proteins. Jonah C., Rao B.M. Radiation Chemistry: Present Status and Future Prospects. 2001;553-584 Elsevier, Amsterdam
18. Jacob J.S., Cistola D.P., Hsu F.F., Muzaffar S., Mueller D.M., Hazen S.L., Heinecke J.W. Human phaghocytes employ the myeloperoxidase-hydrogen peroxide system to synthesize dityrosine, trityrosine, pulcherosine and isodityrosine by a tyrosyl radical-dependent pathway. J. Biol. Chem. 271:1996;19950-19956
19. Kalyanasundaram, K., Thomas, J.K., 1976. Radiation-induced processes in nonionic micelles. In: Proceedings of the Micelle Symposium. Albany, New York, pp. 569-588.
20. Land E.J., Prutz W.A. Reactions of azide radicals with amino acids and proteins. Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 36:1979;75-83
21. Luisi P.L., Magrid L.J. Solubilization of enzymes and nucleic acids in hydrocarbon micellar solutions. CRC Crit. Rev. Biochem. 20:1986;409-474
22. Malencik D.A., Anderson S.R. Dityrosine. preparation, isolation, and analysis Anal. Biochem. 242:1996;202-213
23. Merck Index, 1983.
24. Neta P., Huie R.E., Ross A.B. Rate constants for reactions of inorganic radicals in aqueous solution. J. Phys. Chem. Ref. Data. 17:1988;1027-1284
25. Priyadarsini K.I. Free radical reactions of curcumin in membrane models. Free Radical Biol.Med. 23:1997;838-843
26. Rafikova O., Rafikov R., Nudler E. Catalysis of S-nitrosothiols formation by serum albumin. the mechanism and implication in vascular control Proc. Natl. Acad. Sci. USA. 99:2002;5913-5918
27. Rehfeld S.J. Solubilization of benzene in azqueous sodium dodecyl sulfate solutions measured by differential spectroscopy. J. Phys. Chem. 74:1970;117-122
28. Reiss-Husson F., Luzzati V. The structure of the micellar solutions of some amphiphilic compounds in pure water as determined by absolute small-angle X-ray scattering techniques. J. Phys. Chem. 68:1964;3504-3511
29. Rispens T., Engberts J.B. Micellar catalysis of Diels-Alder reactions. substrate positioning in the micelle J. Org. Chem. 67:2002;7369-7377
30. Spinks J.W.T., Woods R.J. Introduction to Radiation Chemistry. 3rd Edition:1990;Wiley, New York
31. Valdez D., Le Huérou J-Y., Gindre M., Urbach W., Waks M. Hydration and protein folding in water and in reverse micelles. compressibility and volume change Biophys. J. 80:2001;2751-2760
32. Van der Vliet A., Eiserich J.P., O'Neill C.A., Halliwell B., Cross C.E. Tyrosine modification by reactive nitrogen species. a closer look Arch. Biochem. Biophys. 319:1995;341-349
33. Van Montfort R.L., Congreve M., Tisi D., Carr R., Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature. 423:2003;773-777
34. Wheeler O.H., Montalvo R. Radiolysis of phenylalanine and tyrosine and aqueous solutions. Radiat. Res. 40:1969;1-10
35. Wilhelm E., Battino R. Thermodynamic functions of the solubilities of gases in liquids at 25°C. Chem. Rev. 73:1973;1-9
36. Wilhelm E., Battino R., Wilcox J. Low-pressure solubility of gases in liquid water. Chem. Rev. 77:1977;219-262