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- W4251268718 abstract "Oxidants, such as hypochlorous acid (HOCl) and peroxynitrous acid (ONOOH) are under both physiological conditions and as part of the immune response. Proteins are significant targets for these oxidants due to their abundance and high rate constants for reaction, with sulfur-containing amino acids being major targets. Whilst the reaction of oxidants with cysteine and methionine have been widely studies and characterized, reactions at disulfide bonds poorly characterized, and the consequences of these reactions are not well established. Such reactions may be of particular relevance for extracellular proteins and plasma, where disulfide bonds are abundant. That disulfide bonds on proteins are kinetically significant targets for oxidants, with this resulting in the formation of short-lived, reactive thiosulfinates that undergo secondary reactions leading to disulfide bond cleavage and adduct formation. Kinetic analysis indicates that HOCl react with disulfide bonds with rate constants, k, 103 – 107 M-1 s-1. These reactions yield mono-oxygenated, unstable intermediates, assigned as thiosulfinates [RSS(=O)R’]. Further reactions of these species give rise to disulfide bond cleavage, or alternatively reaction with another thiol, such as GSH, to give a glutathionylated protein. Thus, oxidation of alpha-lactalbumin (which contains no free Cys residues) with HOCl or ONOOH yields thiosulfinates (which have a lifetime of many hours) that can react with GSH to give a glutathionylated protein. The latter have been detected by both anti-GSH antibodies and mass spectrometry. Similar reactions with other thiol-containing proteins gives rise to novel protein-protein adducts. Disulfide oxidation can give rise to long-lived oxidants on proteins that can undergo further reaction with thiols, including GSH and other proteins, to give mixed disulfides and protein dimers. These reactions may play a key role in GSH-dependent cell signaling and tissue damage, as well as protein aggregation and dysfunction in disease." @default.
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- W4251268718 date "2018-11-01" @default.
- W4251268718 modified "2023-09-25" @default.
- W4251268718 title "Oxidation of disulfide bonds: a novel pathway to protein glutathionylation" @default.
- W4251268718 doi "https://doi.org/10.1016/j.freeradbiomed.2018.10.085" @default.
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