Dataset Information


Persulfide reactivity in the detection of protein s-sulfhydration.

ABSTRACT: 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.

PROVIDER: S-EPMC3745995 | BioStudies |

REPOSITORIES: biostudies

Similar Datasets

2016-01-01 | S-EPMC4845716 | BioStudies
2018-01-01 | S-EPMC5843340 | BioStudies
2018-01-01 | S-EPMC6159213 | BioStudies
2016-01-01 | S-EPMC4944133 | BioStudies
2019-01-01 | S-EPMC6401616 | BioStudies
2015-01-01 | S-EPMC4470748 | BioStudies
1000-01-01 | S-EPMC4040604 | BioStudies
2019-01-01 | S-EPMC7086210 | BioStudies
2017-01-01 | S-EPMC5863038 | BioStudies
2014-01-01 | S-EPMC3910450 | BioStudies