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Detection of protein S-sulfhydration by a tag-switch technique.

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(.) .

SUBMITTER: Zhang D

PROVIDER: S-EPMC4306352 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

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Detection of protein S-sulfhydration by a tag-switch technique.

Zhang Dehui D Macinkovic Igor I Devarie-Baez Nelmi O NO Pan Jia J Park Chung-Min CM Carroll Kate S KS Filipovic Milos R MR Xian Ming M

Angewandte Chemie (International ed. in English) 20131129 2

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 ...[more]

PMID: 24288186

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Persulfide reactivity in the detection of protein s-sulfhydration.

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