Chloroperoxidase from Caldariomyces fumago

Chloroperoxidase is a heme containing glycoprotein that is secreted from fungus. Chloroperoxidase (CPO) is a extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group.

It has been used to study biocatalytic oxidation in polymersome nanoreactors.

Chloroperoxidase from Caldariomyces fumagois is useful alternative to lactoperoxidase for ¹³¹I ion labeling studies, for bromination of proteins, and for ³⁶Cl labeling of macromolecules in long-term isolation procedures. It has been used to study biocatalytic oxidation in polymersome nanoreactors .

A useful alternative to lactoperoxidase for ¹³¹I ion labeling studies, for bromination of proteins, and for ³⁶Cl labeling of macromolecules in long-term isolation procedures.

Chloroperoxidase (CPO) is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme and it also catalyzes peroxidase, catalase and cytochrome P450-type reactions of dehydrogenation, hydrogenperoxide (H₂O₂) decomposition and oxygen insertion, respectively. The enzyme has magnetic and spectroscopic properties similar to that of cyctochrome P-450. CPO from the fungus Caldariomyces fumago has the capacity to chlorinate aromatic hydrocarbons, including polycyclic aromatic hydrocarbons (PAHs). PAHs are considered to be a potential health risk because of their possible carcinogenic and mutagenic activities and are widely dispersed in the environment.

Crude suspension in 0.1 M sodium phosphate, pH ~4.5

One unit will catalyze the conversion of 1.0 μmole of monochlorodimedon to dichlorodimedon per min at pH 2.75 at 25 °C in the presence of potassium chloride and H₂O₂.