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Chloride peroxidase () is a family of 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:
This enzyme belongs to the family of , specifically those acting on a peroxide as acceptors (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 vanadium. (this paper also discussed chloroperoxidases.
The heme-containing chloroperoxidase (CPO) 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.
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