The oxidative modification of specific cysteine residues to persulfides is thought to be the main way by which hydrogen sulfide (HS) exerts its biological and signaling functions. Therefore, protein persulfidation represents an important thiol-switching mechanism as other reversible redox post-translational modifications. Considering their reductase activity but also their connections with proteins that generate HS and its related molecules, the glutaredoxin (GRX) and thioredoxin (TRX)-reducing systems have potential dual roles in both protein persulfidation and depersulfidation. In this review, we will first focus on recent advances describing the physiological pathways leading to protein persulfidation before discussing the dual roles of the physiological TRX and glutathione/GRX-reducing systems in protein persulfidation/depersulfidation.
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The oxidative modification of specific cysteine residues to persulfides is thought to be the main way by which hydrogen sulfide (HS) exerts its biological and signaling functions. Therefore, protein persulfidation represents an important thiol-switching mechanism as other reversible redox post-translational modifications. Considering their reductase activity but also their connections with proteins that generate HS and its related molecules, the glutaredoxin (GRX) and thioredoxin (TRX)-reducing systems have potential dual roles in both protein persulfidation and depersulfidation.
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