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10.1016/j.chom.2013.07.012 97 SanoT.OzakiK.KodamaY.MatsuuraT.NaramaI

We show (i) that PfGrx-catalyzed redox reactions outcompete uncatalyzed reactions between roGFP2 and GSH or GSSG by several orders of magnitude, (ii) that the PfGrx-catalyzed reduction and oxidation of roGFP2 occur via a mono- and not a dithiol mechanism, and (iii) that the reduction of roGFP2(S 2 ) as a model non-glutathione disulfide substrate most likely involves a rate-limiting glutathionylation in a ternary complex with a GSH molecule that is activated at the 1st glutathione-interaction site of PfGrx

A multivariate analysis

Many people now track visible improvements through glutathione drip comparisons before and after