Thioredoxin antioxidant functions

Mammalian thioredoxin reductases are a family of selenium-containing pyridine nucleotide-disulfide oxidoreductases. These enzymes catalyze NADPH-dependent reduction of the redox protein thioredoxin (Trx), which contains a redox-active disulfide and dithiol group and by itself may function as an efficient cytosolic antioxidant [77]. One of the functions of Trx/ thioredoxin reductase system is the NADPH-catalyzed reduction of protein disulfide [78] ... 

Fernandes, A.P., and Holmgren, A. 2004. Glutaredoxins glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox Signal. 6 63-74. 

Peroxiredoxins Group of antioxidant thioredoxin-dependent enzymes with a catalytic fnnc-tion in the detoxification of cellnlar-toxic peroxides. See Claiborne, A., Ross, R.P., and Parsonage, D., Flavin-linked peroxide rednctases protein-sulfenic acids and the oxidative stress response. Trends Biochem. Sci. 17, 183-186, 1992 Dietz, K-J., Horhing, R, Konig, J., and Baien, M., The function of chloroplast 2-cysteine peroxiredoxin I peroxide detoxification and its regulation, J. Expt. Bot. 53, 1321-1329, 2002 Immenschuh, S. 

As mentioned above, Zn is the most abundant transition metal in cells, and plays a vital role in the functionalities of more than 300 enzymes, in the stabilization of DNA, and in gene expression. Other trace metals, such as Se, W, and Mo, are essential in human health and also important in the environment. For example, Se is usually incorporated into antioxidant enzymes as seleno-cysteine (SeCys), the redox active site of SeCys-containing enzymes, and plays a key role in host oxidative defense. It is predicted that there are a total of 25 SeCys-containing proteins in humans. The most widely known SeCys-containing enzymes are thioredoxin reductase and glutathione peroxidase. Both are ubiquitous and found in bacteria, plants, and mammals, including humans. ... 

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