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Chloride peroxidase is a family of enzymes that catalyzes the chlorination of organic compounds. This enzyme combines the inorganic substrates chloride and hydrogen peroxide to produce the equivalent of Cl, which replaces a proton in hydrocarbon substrate:
In fact the source of "Cl" is hypochlorous acid. Many organochlorine compounds are biosynthesized in this way.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptors. 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 vanadium.
The heme-containing chloroperoxidase exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions. Despite functional similarities with other heme enzymes, the structure of CPO is unique, which folds into a tertiary structure dominated by eight helical segments. The catalytic acid base, required to cleave the peroxide O-O bond, is glutamic acid rather than histidine as in horseradish peroxidase.