Peroxidases are a group of enzymes that catalyze oxidation-reduction reactions. As such, they are classified as oxidoreductases. Toxic molecules such as superoxide and hydroxide radicals can be found in cells due to the presence of oxygen. These are byproducts of aerobic respiration. They are eliminated by a number of enzymes present inside the cell. Superoxide, for example, is destroyed by superoxide dismutase. The degradation, however, produces more hydrogen peroxide (H2O2), which is, in turn, destroyed by peroxidase. Peroxidases reduce H2O2 to water while oxidizing a variety of substrates. Thus, peroxidases are oxidoreductases which use H2O2 as electron acceptor for catalyzing different oxidative reactions.
The overall reaction is as follows:
donor + H2O2 <=> oxidized donor + 2H2O
Some enzymes require the presence of certain molecules, which are not part of their primary structure or amino acid sequence, for their enzymatic activity. These molecules are called cofactors. In peroxidase, the bound cofactor necessary for its activity is heme. Heme is a complex between an iron ion and the molecule protoporphyrin IX.
Origin: erythrocytes, fungal cells (Aspergillus species.)
EC number: 1.11.1.6 |