Significance: Selenenyl sulfides (RSeSRs) and thioseleninic acids (RSeSHs) are the monoselenium (Se) analogs of disulfides and persulfides that contain Se-S bonds. These bonds are found in several antioxidant-regenerating enzymes as derivatives of selenocysteine, making them an important player in redox biology as it pertains to sulfur redox regulation. Recent Advances: Mechanistic studies of redox-regulating selenoenzymes such as thioredoxin reductase and glutathione peroxidase suggest crucial Se-S bonds in the active sites. Peptide models and small-molecule mimics of these active sites have been prepared to study their fundamental chemistry. These advances help pave the road to better understand the functions of the Se-S bond in the body. Critical Issues: The Se-S bond is unstable at atmospheric temperatures and pressures. Therefore, studying their properties proposes a major challenge. Currently, there are no trapping reagents specific to RSeSRs or RSeSHs, making their presence, identity, and fates in biological environments difficult to track. Future Directions: Further understanding of the fundamental chemistry/biochemistry of RSeSRs and RSeSHs is needed to understand what their intracellular targets are and to what extent they impact signaling. Besides antioxidant regeneration and peroxide radical reduction, the roles of RSeSR and RSeSHs in other systems need to be further explored.
Keywords: chemical reaction; reactive sulfur species; selenenyl sulfide; selenocysteine; thioseleninic acid.