Abstract
The kinetics and mechanism of the oxidation of Glycine (Gly), Alanine (Ala), Tyrosine (Tyr), Tryptophan (Trp) and some di-(Gly-Gly, Ala-Ala, Gly-Ala, Gly-Trp, Trp-Gly, Gly-Tyr, Tyr-Gly), tri-(Gly-Gly-Gly, Ala-Gly-Gly) and tetrapeptides (Gly-Gly-Gly-Gly) mediated by sulfate (SO4•−) and hydrogen phosphate (HPO4•−) radicals was studied, employing the flash-photolysis technique. The substrates were found to react with sulfate radicals (SO4•−, produced by photolysis of the S2O82−) faster than with hydrogen phosphate radicals (HPO4•−, generated by photolysis of P2O84− at pH = 7.1). The reactions of the zwitterions of the aliphatic amino acids and peptides with SO4•− radicals take place by electron transfer from the carboxylate moiety to the inorganic radical, whereas those of the HPO4•− proceed by H-abstraction from the α carbon atom. The phenoxyl radical of Tyr-Gly and Gly-Tyr are formed as intermediate species of the oxidation of these peptides by the inorganic radicals. The radical cations of Gly-Trp and Trp-Gly (at pH = 4.2) and their corresponding deprotonated forms (at pH = 7) were detected as intermediates species of the oxidation of these peptides with SO4•− and HPO4•−. Reaction mechanisms which account for the observed intermediates are proposed.
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Bosio, G., Criado, S., Massad, W. et al. Kinetics of the interaction of sulfate and hydrogen phosphate radicals with small peptides of glycine, alanine, tyrosine and tryptophan. Photochem Photobiol Sci 4, 840–846 (2005). https://doi.org/10.1039/b507856c
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DOI: https://doi.org/10.1039/b507856c