Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation.

Hydrogen sulfide (HS) has emerged as a signalling molecule capable of regulating several important physiological functions such as blood pressure, neurotransmission and inflammation. The mechanisms behind these effects are still largely elusive and oxidative posttranslational modification of cysteine residues (protein persulfidation or -sulfhydration) has been proposed as the main pathway for HS-induced biological and pharmacological effects. As a signalling mechanism, persulfidation has to be controlled.