Abstract

The research area of persulfides and polysulfides has piqued the interest of many scientists worldwide. Numerous attempts have been made to understand the nature of reactive sulfur species particularly biological polysulfides and supersulfides (RSnSH). Appreciable amounts of the endogenous RSnSH cysteine hydropersulfide were discovered in various organisms. The moonlighting function of mitochondrial cysteinyl-tRNA synthetase as a persulfide synthase was also discovered. This enzyme was thought to be the major player in the biogenesis of endogenous low-molecular-weight RSnSH, and, as one important function, it integrates RSnSH into proteins. Several studies indicated that RSnSH is highly relevant to various biological functions, from cell signaling to electrophilic regulation. In this review, we focus on highlighting the potential roles of endogenous RSnSH as part of the critical biological detoxification mechanism.

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