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The kinetic data can be best explained by a ternary complex in which PfGrx recruits and activates GSH at the 1st glutathione-interaction site to facilitate the rate-limiting glutathionylation of roGFP2 WT (S 2 ) and its subsequent deglutathionylation in accordance with monothiol mechanism (iii) from Fig

PCC6803, a MerA-like enzyme that functions in mercury and uranium reduction was shown to be redox-controlled by S -glutathionylation (Marteyn et al., 2013)

It is a chemical inhibitor of the enzyme nicotinamide N-methyltransferase (NNMT), which catalyzes the methylation of nicotinamide using S-adenosylmethionine as the methyl donor