Biochem/physiol Actions
Each subunit of the tetramer contains iron bound to a protoheme IX group. The enzyme also strongly binds NADP, which is in close proximity to the heme group. Catalase activity is constant over the pH range of 4.0-8.5. The pI is found to be 5.4. Optimum pH for catalytic activity is 7.0. The enzyme activity is inhibited by 3-amino-1-H-1,2,4 triazole, cyanide, azide, hydroxylamine, cyanogen bromide, 2-mercaptoethanol, dithiothreitol, dianisidine, and nitrate. Incubation of catalase with ascorbate or ascorbate/Cu2+ results in degradation of the catalase molecule.
Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis.
Unit Definition
One unit will decompose 1.0 μmole of H2O2 per min at pH 7.0 at 25 °C, while the H2O2 conc. falls from 10.3 to 9.2 mM, measured by the rate of decrease of A240.