Glutathione peroxidase heme-containing

Peroxidases (E.C. 1.11.1.7) are ubiquitously found in plants, microorganisms and animals. They are either named after their sources, for example, horseradish peroxidase and lacto- or myeloperoxidase, or akin to their substrates, such as cytochrome c, chloro- or lignin peroxidases. Most of the peroxidases studied so far are heme enzymes with ferric protoporphyrin IX (protoheme) as the prosthetic group (Fig. 1). However, the active centers of some peroxidases also contain selenium (glutathione peroxidase) [7], vanadium (bromoperoxidase)... 

Selenium is an essential trace element and an integral component of heme oxidase. It appears to augment the antioxidant action of vitamin E to protect membrane lipids from oxidation. The exact mechanism of this interaction is not known however, selenium compounds are found in the selenium analogs of the sulfur-containing amino acids, such as cysteine and methionine. Se-cysteine is found in the active sites of the enzyme glutathione peroxidase, which acts to use glutathione to reduce organic hydroperoxides. 

Most peroxidases are heme enzymes and contain the ferric protoporphyrin IX (protoheme) group with an iron atom in their active center (Fig. 1). Only a few other peroxidases known so far have other metal centers and/or different prosthetic groups. Glutathione peroxidase, for example, has a selen-... 

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