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Investigations have highlighted many roles in which it is used including antioxidant defense, detoxification of electrophilic xenobiotics, modulation of redox regulated signal transduction, storage and transport of cysteine, regulation of cell proliferation, synthesis of deoxyribonucleotide synthesis, regulation of immune responses, and regulation of leukotriene and prostaglandin metabolism[13]

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Under S-glutathionylation, GSH may bind to cysteinyl residues in proteins by creating reversible disulfide bonds, depending on the cysteine position and redox potential [66,67]

However, to date, no structural data is available in order to elucidate the orientation of HQ in the active site of tyrosinase