The use of genetically encoded redox sensors in phagocytized bacteria reveals that, among the toxic cocktail of oxidants released into the neutrophil's phagolysosome, HOCl is the main component responsible for the oxidative modification of bacterial protein thiols.
The chloroplast 2-cysteine peroxiredoxin is central player and missing link in the chloroplast thiol-disulfide redox regulatory network, and participates in oxidative inactivation of reductively activated enzymes in photosynthesis.
ATF4, the master regulator of transcription during the Integrated Stress Response (ISR), causes global changes in cysteine sulfhydration of proteins and this event causes cellular metabolic reprogramming.
The common post-translational modification trans-4-hydroxy-L-proline is reversed by gut microbes with the help of hydroxyproline dehydratase (HypD), an enzyme that performs a radical chemical mechanism.
The regulatory switch from protection to assimilation, which plants use to exploit natural, fluctuating light, involves movement of the enzyme ferredoxin:NADP(H) oxidoreductase between chloroplast membrane complexes.