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Redox pathways are involved in several processes in biology, such as signal transduction, regulation of gene expression, oxidative stress and energy metabolism. Proteins are the central mediators of electron transfer processes. Many of these proteins rely on nonproteinaceous redox cofactors (such as NAD+; FAD; heme; or Cu, Fe or other transition metals) for their redox activity. In contrast, other proteins use cysteine residues for this property (Netto et al., 2007). The amino acid cysteine has low reactivity for redox transitions (Winterbourn and Metodiewa, 1999; Wood et al., 2003; Marino and Gladishev, 2011). However, protein folding can generate environments in which cysteine residues are reactive. Examples are reduction (or isomerization or formation) of disulfide bonds, reduction of methionine thioesther-sulfoxide, degradation of peptide bonds, peroxide reduction, and others (Lindahl et al., 2011).

Site-Directed Mutagenesis as a Tool to Characterize Specificity in Thiol-Based Redox Interactions Between Proteins and Substrates