Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity (PubMed:11875065, PubMed:12684511). The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX2 is more active as an oxidoreductase than GRX1 (PubMed:9571241, PubMed:18992757, PubMed:20417731). Responsible for the S-glutathionylation of DHBP synthase (PubMed:21565288). 2 glutathione + H2O2 = glutathione disulfide + 2 H2O 1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+) glutathione + RX = a halide anion + an S-substituted glutathione + H(+) In response to exposure to reactive oxygen species (ROS) and upon entry into stationary phase. Present with 31400 molecules/cell in log phase SD medium. It is unclear whether the long polypeptide observed in mitochondria represents the immature form of the protein before cleavage of the transit peptide and release of the short form into the cytoplasm or whether two mature isoforms exists. Belongs to the glutaredoxin family. Truncated N-terminus.