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Last Updated: 3 years ago

Possible Interaction: Cysteine and Hydrogen Peroxide

Research Papers that Mention the Interaction

Focusing on three ER-localized proteins—the molecular chaperone BiP, the transmembrane stress-sensor IRE1, and the calcium pump SERCA2—we discuss how post-translational modification of protein cysteines by H2O2 can alter ER activities.
Cells  •  2020  |  View Paper
The cysteines of most H2O2 effectors are therefore at a competitive disadvantage for reaction with H2O2.
Antioxidants & redox signaling  •  2018  |  View Paper
PYK2 downregulation, l-cysteine supplementation, or CSE overexpression alleviated the effects of H2O2 on H9c2 cardiomyocyte survival.
Molecular Pharmacology  •  2017  |  View Paper
Given that Prxs are abundant and possess a structure that renders the cysteine (Cys) residue at the active site highly sensitive to oxidation by H2O2 , the signaling function of this oxidant requires extensive and highly localized regulation.
Annual review of biochemistry  •  2017  |  View Paper
Here, we report that hydrogen peroxide heightens endocannabinoid signaling in brain neurons through sulfenylation of cysteines C201 and C208 in monoacylglycerol lipase (MGL), a serine hydrolase that deactivates the endocannabinoid 2-arachidonoyl-sn-glycerol (2-AG) in nerve terminals.
Chemistry & biology  •  2015  |  View Paper
Peroxiredoxins (Prxs) contain an active site cysteine that is sensitive to oxidation by H2O2.
The Journal of Biological Chemistry  •  2011  |  View Paper
Pretreatment with hydrogen peroxide , l‐aspartic acid β‐hydroxamate or 1‐methyl‐4‐phenylpyridinium reduced the subsequent cysteine increase in midbrain slice cultures.
The European journal of neuroscience  •  2008  |  View Paper
3-Mercaptopyruvate sulfurtransferase serves as an antioxidant protein: when the enzyme is exposed to stoichiometric amounts of the oxidant hydrogen peroxide , it is inhibited via the formation of low redox sulfenate at the catalytic site cysteine.
Current medicinal chemistry  •  2006  |  View Paper
This suppressive effect of H2O2 could be relieved by reducing agents (dithiothreitol and cysteine).
Journal of neurochemistry  •  2003  |  View Paper
Specifically, H2O2 appears to oxidize active site cysteines in phosphatases, thereby inactivating them.
Science's STKE  •  2000  |  View Paper
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