Glutathionylation disulfides

Huang, K. P. and Huang, F. L. (2002) Glutathionylation of proteins by glutathione disulfide S-oxide. Biochem. Pharmacol. 64, 1049-1056. 

Figure 2. The incubation in the presence of GSSG induces the S-glutathionylation of c-Jun and an inhibition in its DNA binding activity. A) The DNA binding of c-Jun was subjected to EMSA experiments in the presence of different GSH/GSSG ratios or DTT. B) In the figure is represented the amount of c-Jun protein which is modified to mixed disulfide with glutathione (P-S-S-G) or to other modifications.

Reddy S, Jones AD, Cross CE, Wong PS, Van Der Vliet A (2000) Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue. Biochem J 347 821-7 Holmgren A (1990) Glutaredoxin structure and function. In Vina J (ed) Glutathione metabolism and physiological functions. CRC, Boca Raton, Florida, pp 145-15430 Holmgren A (1984) Enzymatic reduction-oxidation of protein disulfides by thiore-doxin. Methods Enzymol 107 295-300... 

Decker CJ, Cashman JR, Sugiyama K, Maltby D, Correia MA (1991) Formation of glutathionyl-spi-ronolactone disulfide by rat liver cytochromes P450 or hog liver flavin-containing monooxygenases a functional probe of two-electron oxidations of the thiosteroid Chem Res Toxicol 4 6694577... 

The sulfhydryl group of the Cys residue can form a covalent disulfide bond with another sulfhydryl. The other sulfhydryl may be from another Cys residue in the same protein, or from a small molecule such as glutathione or free cysteine (glutathionylation or cysteinylation). The formation of disulfide bonds in specific configurations is often important to the structure, function, or stability of the biopharmaceutical protein. Therefore, the confirmation of the disulfide connectivity is necessary. The analysis of disulfide bond structure is discussed in more detail in Section II.A.2. 

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