Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 53, Issue 2, Pages 575-581Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201305876
Keywords
hydrogen sulfide; protein S-sulfhydration; signal transduction; tag-switch; thiols
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Funding
- NSF-CAREER Program [0844931]
- American Chemical Society
- University of Erlangen-Nuremberg within Emerging Field Initiative (EFI-MRIC)
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0844931] Funding Source: National Science Foundation
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Protein S-sulfhydration (forming -S-SH adducts from cysteine residues) is a newly defined oxidative posttranslational modification and plays an important role in H2S-mediated signaling pathways. In this study we report the first selective, tag-switch method which can directly label protein S-sulfhydrated residues by forming stable thioether conjugates. Furthermore we demonstrate that H2S alone cannot lead to S-sulfhydration and that the two possible physiological mechanisms include reaction with protein sulfenic acids (P-SOH) or the involvement of metal centers which would facilitate the oxidation of H2S to HS..
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