Journal article
Detection of protein S-sulfhydration by a tag-switch technique
Angewandte Chemie (International ed.), Vol.53(2), pp.575-581
01/07/2014
Handle:
https://hdl.handle.net/2376/106976
PMCID: PMC4306352
PMID: 24288186
Abstract
Protein S-sulfhydration (forming -S-SH adducts from cysteine residues) is a newly defined oxidative posttranslational modification and plays an important role in H2 S-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 H2 S 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 H2 S to HS(.) .
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Details
- Title
- Detection of protein S-sulfhydration by a tag-switch technique
- Creators
- Dehui Zhang - Department of Chemistry, Washington State University, Pullman, WA 99164 (USA)Igor MacinkovicNelmi O Devarie-BaezJia PanChung-Min ParkKate S CarrollMilos R FilipovicMing Xian
- Publication Details
- Angewandte Chemie (International ed.), Vol.53(2), pp.575-581
- Academic Unit
- Chemistry, Department of
- Publisher
- Germany
- Grant note
- R01 GM102187 / NIGMS NIH HHS R01 CA174864 / NCI NIH HHS
- Identifiers
- 99900546866101842
- Language
- English
- Resource Type
- Journal article