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. Author manuscript; available in PMC: 2018 Mar 1.
Published in final edited form as: Arch Biochem Biophys. 2016 Sep 28;617:26–37. doi: 10.1016/j.abb.2016.09.013

Figure 2.

Figure 2

Figure 2

Figure 2

Figure 2

A proposed mechanism for enzymatic glutathionylation of target signaling proteins by peroxiredoxin (Prx), glutathione S-transferase π (GST), or glutaredoxin (Grx). Similar reactions may also occur with GPx. In (A), 1- H2O2 oxidized Prx; 2- GSH forms a disulfide with Prx; 3- disulfide exchange occurs with the target protein thiolate. In (B), steps 2 and 3 are in reverse sequence from (A). In (C), 1- GSSG, which must be formed by a closely associated peroxidase undergoes disulfide exchange with the thiolate in the active site of GST π; 2- disulfide exchange occurs with the target protein thiolate. In (D), GSSG, which must be formed by a closely associated peroxidase undergoes disulfide exchange with the thiolate in the active site of Grx; 2- An intramolecular disulfide forms in the active site of Grx; 3- disulfide exchange occurs with the target protein thiolate; 4- disulfide exchange occurs with GSH.