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- W2017144791 abstract "The intramolecular reaction of cysteine thiyl radicals with peptide and protein αC−H bonds represents a potential mechanism for irreversible protein oxidation. Here, we have measured absolute rate constants for these reversible hydrogen transfer reactions by means of pulse radiolysis and laser flash photolysis of model peptides. For N-Ac-CysGly6 and N-Ac-CysGly2AspGly3, Cys thiyl radicals abstract hydrogen atoms from Gly with kf = (1.0−1.1) × 105 s−1, generating carbon-centered radicals, while the reverse reaction proceeds with kr = (8.0−8.9) × 105 s−1. The forward reaction shows a normal kinetic isotope effect of kH/kD = 6.9, while the reverse reaction shows a significantly higher normal kinetic isotope effect of 17.6, suggesting a contribution of tunneling. For N-Ac-CysAla2AspAla3, cysteine thiyl radicals abstract hydrogen atoms from Ala with kf = (0.9−1.0) × 104 s−1, while the reverse reaction proceeds with kr = 1.0 × 105 s−1. The order of reactivity, Gly > Ala, is in accord with previous studies on intermolecular reactions of thiyl radicals with these amino acids. The fact that kf < kr suggests some secondary structure of the model peptides, which prevents the adoption of extended conformations, for which calculations of homolytic bond dissociation energies would have predicted kf > kr. Despite kf < kr, model calculations show that intramolecular hydrogen abstraction by Cys thiyl radicals can lead to significant oxidation of other amino acids in the presence of physiologic oxygen concentrations." @default.
- W2017144791 created "2016-06-24" @default.
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- W2017144791 date "2008-10-31" @default.
- W2017144791 modified "2023-10-03" @default.
- W2017144791 title "Reversible Intramolecular Hydrogen Transfer between Cysteine Thiyl Radicals and Glycine and Alanine in Model Peptides: Absolute Rate Constants Derived from Pulse Radiolysis and Laser Flash Photolysis" @default.
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- W2017144791 doi "https://doi.org/10.1021/jp805133u" @default.
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