Polysulfides link H2S to protein thiol oxidation.

@article{Greiner2013PolysulfidesLH,
  title={Polysulfides link H2S to protein thiol oxidation.},
  author={Romy Greiner and Zolt{\'a}n P{\'a}link{\'a}s and Katrin B{\"a}sell and D{\"o}rte Becher and Haike Antelmann and P{\'e}ter Nagy and Tobias P Dick},
  journal={Antioxidants & redox signaling},
  year={2013},
  volume={19 15},
  pages={1749-65}
}
AIMS Hydrogen sulfide (H2S) is suggested to act as a gaseous signaling molecule in a variety of physiological processes. Its molecular mechanism of action was proposed to involve protein S-sulfhydration, that is, conversion of cysteinyl thiolates (Cys-S(-)) to persulfides (Cys-S-S(-)). A central and unresolved question is how H2S-that is, a molecule with sulfur in its lowest possible oxidation state (-2)-can lead to oxidative thiol modifications. RESULTS Using the lipid phosphatase PTEN as a… CONTINUE READING
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