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Reactivity of bovine whey proteins, peptides, and amino acids toward triplet riboflavin as studied by laser flash photolysis.

Authors
Type
Published Article
Journal
Journal of agricultural and food chemistry
Publication Date
Volume
52
Issue
21
Pages
6602–6606
Identifiers
PMID: 15479029
Source
Medline
License
Unknown

Abstract

The reaction between the triplet excited state of riboflavin and amino acids, peptides, and bovine whey proteins was investigated in aqueous solution in the pH range from 4 to 9 at 24 degrees C using nanosecond laser flash photolysis. Only tyrosine and tryptophan (and their peptides) were found to compete with oxygen in quenching the triplet state of riboflavin in aqueous solution, with second-order rate constants close to the diffusion limit, 1.75 x 10(9) and 1.40 x 10(9) L mol(-1) s(-1) for tyrosine and tryptophan, respectively, with beta-lactoglobulin and bovine serum albumin having comparable rate constants of 3.62 x 10(8) and 2.25 x 10(8) L mol(-1) s(-1), respectively. Tyrosine, tryptophan, and their peptides react with the photoexcited triplet state of riboflavin by electron transfer from the tyrosine and tryptophan moieties followed by a fast protonation of the resulting riboflavin anion rather than by direct H-atom abstraction, which could be monitored by time-resolved transient absorption spectroscopy as a decay of triplet riboflavin followed by a rise in riboflavin anion radical absorption. For cysteine- and thiol-containing peptides, second-order rate constants depend strongly on pH, for cysteine corresponding to pKaRSH = 8.35. H-atom abstraction seems to operate at low pH, which with rising pH gradually is replaced by electron transfer from the thiol anion. From the pH dependence of the second-order rate constant, the respective values for the H-atom abstraction (k = 1.64 x 10(6) L mol(-1) s(-1)) and for the electron transfer (k = 1.20 x 10(9) L mol(-1) s(-1)) were determined.

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