chloroperoxidáza

Chloroperoxidase is an enzyme found in certain species of fungi, most notably in the genus *Caldariomyces*. It is a heme-containing enzyme that catalyzes a variety of oxidative halogenation reactions. This enzyme is unique in that it possesses both peroxidase and halogenase activity within a single polypeptide chain. It requires a heme prosthetic group for its catalytic function.

The primary function of chloroperoxidase is the oxidation of chloride ions in the presence of hydrogen peroxide, leading to the formation of hypochlorous acid. This hypochlorous acid can then be used by the fungus for various purposes, including the synthesis of organochlorine compounds. These compounds can serve as antimicrobial agents, aiding the fungus in its ecological niche. The enzyme's active site is thought to be accessible to both halide ions and organic substrates, facilitating its diverse catalytic capabilities.

Beyond chlorination, chloroperoxidase can also catalyze bromination and iodination reactions, depending on the available halide ions. It can also perform peroxygenation reactions, similar to other peroxidases. The enzyme's ability to operate under a wide range of pH conditions and its stability make it a subject of interest for biotechnological applications, such as in bioremediation and the synthesis of halogenated organic compounds. Research continues to explore the full enzymatic repertoire and potential uses of chloroperoxidase.