The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Persulfide Reactivity in the Detection of Protein S-Sulfhydration
Open accessAbstract
Hydrogen sulfide (H2S) has emerged as a new member of the gaseous transmitter family of signaling molecules and appears to play a regulatory role in the cardiovascular and nervous systems. Recent studies suggest that protein cysteine S-sulfhydration may function as a mechanism for transforming the H2S signal into a biological response. However, selective detection of S-sulfhydryl modifications is challenging since the persulfide group (RSSH) exhibits reactivity akin to other sulfur species, especially thiols. A modification of the biotin switch technique, using S-methyl methanethiosulfonate (MMTS) as an alkylating reagent, was recently used to identify a large number of proteins that may undergo S-sulfhydration, but the underlying mechanism of chemical detection was not fully explored. To address this key issue, we have developed a protein persulfide model and analogue of MMTS, S-4-bromobenzyl methanethiosulfonate (BBMTS). Using these new reagents, we investigated the chemistry in the modified biotin switch method and examined the reactivity of protein persulfides toward different electrophile/nucleophile species. Together, our data affirm the nucleophilic properties of the persulfide sulfane sulfur and afford new insights into protein S-sulfhydryl chemistry, which may be exploited in future detection strategies.
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Cites
The reaction of H2S with oxidized thiols: generation of persulfides and implications to H2S biology
Francoleon, N. E., Carrington, S. J., & Fukuto, J. M. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.09.015 · Cited by 199
Cited by
Chemical Biology of H2S Signaling through Persulfidation
Filipovic, M. R., Zivanovic, J., Alvarez, B., & Banerjee, R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00205 · Cited by 1,046
Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling
Ida, T., Sawa, T., Ihara, H., Tsuchiya, Y., Watanabe, Y., Kumagai, Y., Suematsu, M., Motohashi, H., Fujii, S., Matsunaga, T., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321232111 · Cited by 934
Physiological roles of hydrogen sulfide in mammalian cells, tissues, and organs
Cirino, G., Szabo, C., & Papapetropoulos, A. (2023) · Physiological Reviews · doi:10.1152/physrev.00028.2021 · Cited by 553
Ono, K., Akaike, T., Sawa, T., Kumagai, Y., Wink, D. A., Tantillo, D. J., Hobbs, A. J., Nagy, P., Xian, M., Lin, J., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.007 · Cited by 422
Hydrogen sulfide (H2S) releasing agents: chemistry and biological applications
Zhao, Y., Biggs, T. D., & Xian, M. (2014) · Chem. Commun. · doi:10.1039/c4cc00968a · Cited by 358
Cuevasanta, E., Lange, M., Bonanata, J., Coitiño, E. L., Ferrer-Sueta, G., Filipovic, M. R., & Alvarez, B. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.672816 · Cited by 344
Dóka, É., Pader, I., Bíró, A., Johansson, K., Cheng, Q., Ballagó, K., Prigge, J. R., Pastor-Flores, D., Dick, T. P., Schmidt, E. E., et al. (2016) · Science Advances · doi:10.1126/sciadv.1500968 · Cited by 326
Aroca, A., Benito, J. M., Gotor, C., & Romero, L. C. (2017) · Journal of Experimental Botany · doi:10.1093/jxb/erx294 · Cited by 320
Detection of Protein S‐Sulfhydration by a Tag‐Switch Technique
Zhang, D., Macinkovic, I., Devarie‐Baez, N. O., Pan, J., Park, C., Carroll, K. S., Filipovic, M. R., & Xian, M. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201305876 · Cited by 287
Self-citationH2S and its role in redox signaling
Kabil, O., Motl, N., & Banerjee, R. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.01.002 · Cited by 240
Kramer, P. A., Duan, J., Qian, W.-J., & Marcinek, D. J. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00347 · Cited by 54
Metadata
- Authors
- Pan, J., & Carroll, K. S.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-04-12
- Volume
- 8
- Issue
- 6
- Pages
- 1110-1116
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- OpenAlex
- W2169784612
- Cited by
- 185
- References
- 1
- FWCI
- 8.44
- Type
- journal article
- Language
- en
- Open access
- green
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