Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1925674 | Archives of Biochemistry and Biophysics | 2011 | 8 Pages |
Hydrogen sulfide is an endogenously generated molecule with many reported physiological functions. Although several biological targets have been proposed, the biochemical mechanisms by which it elicits activity are not established. Thus, in an effort to begin to delineate the fundamental biological chemistry of H2S, we have examined the reaction of H2S with oxidized thiols and thiol proteins in order to determine whether persulfide formation occurs, is stable and how this may affect protein function. We have found that persulfides are easily generated, relatively stable and can alter enzyme activity. Moreover, we have begun to develop methodology for in situ generation of persulfides to facilitate further study of this potentially important species.
► Reaction of H2S with oxidized thiols results in persulfide formation. ► Persulfides are stable and react as reductants and nucleophiles. ► Persulfide formation in proteins changes their activity. ► Persulfides can be made using DTNB/H2S.