Chloroperoxidase

About Chloroperoxidase

In enzymology, a chloride peroxidase (EC 1.11.1.10) is an enzyme that catalyzes the chemical reaction 2 RH + 2 Cl- + H2O2 \rightleftharpoons 2 RCl + 2 H2O

The 3 substrates of this enzyme are RH, Cl−, and H2O2, whereas its two products are RCl and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is chloride: hydrogen-peroxide oxidoreductase. This enzyme is also called chloroperoxidase. It employs one cofactor which may be either heme or vanadia.

Chloroperoxidases are heme or vanadium-containing enzymes that exhibits peroxidase, catalase and cyto-chrome P450-like activities in addition to catalyzing halogenation reactions[1]. Despite functional similarities with other heme enzymes, CPO folds into a novel tertiary structure dominated by eight helical segments. The catalytic base, required to cleave the peroxide O-O bond, is glutamic acid rather than histidine as in other peroxidases.