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One main finding on the structural side is that the glutathione-hosting site is highly conserved, and uses the negatively charged carboxylate functions of the glycine and glutamic acid residues of glutathione as anchors for substrate recognition by positively charged amino acid residues, as well as negatively charged residues to hold the protonated amino group of the glutamic acid residue

S-glutathionylation modification mediated by hyposulfenamide intermediates

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