Abstract
Thioredoxin (Trx), a ubiquitous protein in organisms, exhibits a highly conserved active site in which two cysteines are separated in the primary structure only by two amino acid residues (CXXC). These cysteine residues can be in the oxidized (disulfide, S-S) or the reduced state (thiols, SH) and enable the Trx function in hydrogen peroxide (H2O2) metabolism and a diversity of interaction…