Chemical Research in Toxicology · 2020 · 30 citations · 46 references
Life SciencesBiochemistryMolecular BiologyApoptosisEnzymologyRedox BiochemistryAntioxidant DefenseDisulfide Bond FormationMolecular Mechanisms Of ToxicityCysteine CatalysisCysteine OxidationDisulfide Bond CleavageElectrophile-protein InteractionsEscherichia ColiPhysiological Stress ResponsesReactive Electrophile SpeciesThiols Protecting Groups
Hydropersulfide and polysulfide species have recently been shown to elicit a wide variety of biological and physiological responses. In this study, we examine the effects of cysteine trisulfide (Cys-SSS-Cys; also known as thiocystine) treatment on E. coli. Previous studies in mammalian cells have shown that Cys-SSS-Cys treatment results in protection from the electrophiles. Here, we show that the protective effect of Cys-SSS-Cys treatment against electrophile-induced cell death is conserved in E. coli. This protection correlates with the rapid generation of cysteine hydropersulfide (Cys-SSH) in the culture media. We go on to demonstrate that an exogenous phosphatase expressed in E. coli, containing only a single catalytic cysteine, is protected from electrophile-induced inactivation in the presence of hydropersulfides. These data together demonstrate that E. coli can utilize Cys-SSS-Cys to generate Cys-SSH and that the Cys-SSH can protect cellular thiols from reactivity with the electrophiles.
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Selective Modification of Glutathione Metabolism
Alton Meister · Science · 1983 · 1.3K citations
Reversible Inactivation of the Tumor Suppressor PTEN by H2O2
Seung-Rock Lee, Kap‐Seok Yang, Jaeyul Kwon et al. · Journal of Biological Chemistry · 2002 · 1K citations · Full text