Sulfane sulfur is common inside cells, playing both regulatory and antioxidant roles. However, there are unresolved issues about its chemistry and biochemistry. We report the discovery that reactive sulfane sulfur such as polysulfides and persulfides could be detected by using resonance synchronous spectroscopy (RS 2 ). With RS 2 , we showed that inorganic polysulfides at low concentrations were unstable with a half-life about 1 min under physiological conditions due to reacting with glutathione. The protonated form of glutathione persulfide (GSSH) was electrophilic and had RS 2 signal. GSS − was nucleophilic, prone to oxidation, but had no RS 2 signal. Using this phenomenon, p K a of GSSH was determined as 6.9. GSSH/GSS − was 50-fold more reactive than H 2 S/HS − towards H 2 O 2 at pH 7.4, supporting reactive sulfane sulfur species like GSSH/GSS − may act as antioxidants inside cells. Further, protein persulfides were shown to be in two forms: at pH 7.4 the deprotonated form (R-SS - ) without RS 2 signal was not reactive toward sulfite, and the protonated form (R-SSH) in the active site of a rhodanese had RS 2 signal and readily reacted with sulfite to produce thiosulfate. These data suggest that RS 2 of sulfane sulfur is likely associated with its electrophilicity. Sulfane sulfur showed species-specific RS 2 spectra and intensities at physiological pH, which may reveal the relative abundance of a reactive sulfane sulfur species inside cells.
Sulfane sulfur has been recognized as a common cellular component, participating in regulating enzyme activities and signaling pathways. However, the quantification of total sulfane sulfur in biological samples is still a challenge. Here, we developed a method to address the need. All tested sulfane sulfur reacted with sulfite and quantitatively converted to thiosulfate when heated at 95 °C in a solution of pH 9.5 for 10 min. The assay condition was also sufficient to convert total sulfane sulfur in biological samples to thiosulfate for further derivatization and quantification. We applied the method to detect sulfane sulfur contents at different growth phases of bacteria, yeast, mammalian cells, and zebrafish. Total sulfane sulfur contents in all of them increased in the early stage, kept at a steady state for a period, and declined sharply in the late stage of the growth. Sulfane sulfur contents varied in different species. For Escherichia coli, growth media also affected the sulfane sulfur contents. Total sulfane sulfur contents from different organs of mouse and shrimp were also detected, varying from 1 to 10 nmol/(mg of protein). Thus, the new method is suitable for the quantification of total sulfane sulfur in biological samples.
Sulfur-oxidizing bacteria can oxidize hydrogen sulfide (H 2 S) to produce sulfur globules. Although the process is common, the pathway is unclear. In recombinant Escherichia coli and wild-type Corynebacterium vitaeruminis DSM20294 with SQR but no enzymes to oxidize zero valence sulfur, SQR oxidized H 2 S into short-chain inorganic polysulfide (H 2 S n , n≥2) and organic polysulfide (RS n H, n≥2), which reacted with each other to form long-chain GS n H (n≥2) and H 2 S n before producing octasulfur (S 8 ), the main component of elemental sulfur. GS n H also reacted with GSH to form GSnG (n≥2) and H 2 S; H 2 S was again oxidized by SQR. After GSH was depleted, SQR simply oxidized H 2 S to H 2 S n , which spontaneously generated S 8 . S 8 aggregated into sulfur globules in the cytoplasm. The results highlight the process of sulfide oxidation to S 8 globules in the bacterial cytoplasm and demonstrate the potential of using heterotrophic bacteria with SQR to convert toxic H 2 S into relatively benign S 8 globules. IMPORTANCE Our results support a process of H 2 S oxidation to produce octasulfur globules via SQR catalysis and spontaneous reactions in the bacterial cytoplasm. Since the process is an important event in geochemical cycling, a better understanding facilitates further studies and provides theoretical support for using heterotrophic bacteria with SQR to oxidize toxic H 2 S into sulfur globules for recovery.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.