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Sulfur-containing amino acids (SAAs) like cysteine and methionine form disulfide bonds and undergo reversible S-glutathionylation, S-nitrosylation, and S-persulfidation that contribute to peroxidase, dehydroascorbate reductase, and transcription factor activity, thereby stabilizing the glutathione-to-glutathione disulfide (GSSG) redox couple

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This substitution promotes an abnormal salt bridge between the N-terminal and C-terminal domains, causing structural changes and altering the protein's folding and conformation