Journal
MOLECULES
Volume 19, Issue 8, Pages 12789-12813Publisher
MDPI
DOI: 10.3390/molecules190812789
Keywords
cystamine; cystathionine gamma-lyase (gamma-cystathionase); garlic; glutathione persulfide; hydrogen sulfide; mercaptoethanol; perseleno selenium; persulfide; sulfane sulfur; thioglycerol
Funding
- NIH [RO1 DK 16739]
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The understanding of sulfur bonding is undergoing change. Old theories on hypervalency of sulfur and the nature of the chalcogen-chalcogen bond are now questioned. At the same time, there is a rapidly expanding literature on the effects of sulfur in regulating biological systems. The two fields are inter-related because the new understanding of the thiosulfoxide bond helps to explain the newfound roles of sulfur in biology. This review examines the nature of thiosulfoxide (sulfane, S-0) sulfur, the history of its regulatory role, its generation in biological systems, and its functions in cells. The functions include synthesis of cofactors (molybdenum cofactor, iron-sulfur clusters), sulfuration of tRNA, modulation of enzyme activities, and regulating the redox environment by several mechanisms (including the enhancement of the reductive capacity of glutathione). A brief review of the analogous form of selenium suggests that the toxicity of selenium may be due to over-reduction caused by the powerful reductive activity of glutathione perselenide.
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