Chloride peroxidase
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.As of late 2007, 30 structures have been solved for this class of enzymes, with PDB accession codes,,,,,,,,,,,,,,,,,,,,,,,,,,,,, and.
