RTI uses cookies to offer you the best experience online. By clicking “accept” on this website, you opt in and you agree to the use of cookies. If you would like to know more about how RTI uses cookies and how to manage them please view our Privacy Policy here. You can “opt out” or change your mind by visiting: http://optout.aboutads.info/. Click “accept” to agree.
Detection of protein S-sulfhydration via a tag-switch technique
Zhang, D., Macinkovic, I., Devarie-Baez, N. O., Pan, J., Park, C.-M., Carroll, K. S., Filpovic, M. R., & Xian, M. (2013). Detection of protein S-sulfhydration via a tag-switch technique. Angewandte Chemie - International Edition, 53(2), 575–581. https://doi.org/10.1002/anie.201305876
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 HSC.