Haloperoxidase
Haloperoxidases are peroxidases that are able to mediate the oxidation of halides by hydrogen peroxide. Both halides and hydrogen peroxide are widely available in the environment.
The Nernst equation shows that hydrogen peroxide can oxidize chloride, bromide and iodide from a thermodynamic perspective under natural conditions, i.e., a temperature range of about 0–30 °C and a pH ranging from about 3 to about 8. Fluoride cannot be oxidized by hydrogen peroxide.
Classification
The table shows the classification of haloperoxidases according to the halides whose oxidation they are able to catalyze.The classification of these enzymes by substrate-usability does not necessarily indicate enzyme substrate preference. For example, although eosinophil peroxidase is able to oxidize chloride, it preferentially oxidizes bromide.
The mammalian haloperoxidases myeloperoxidase, lactoperoxidase and eosinophil peroxidase are also capable of oxidizing the pseudohalide thiocyanate. They each contain a heme prosthetic group covalently bound by two ester linkages to aspartate and/or glutamate side-chains. MPO has a third covalent link through a methionine residue. Horseradish peroxidase is also capable of oxidizing these substrates, but its heme is not covalently bound and becomes damaged during turnover.
A specific vanadium bromoperoxidase in marine organisms uses vanadate and hydrogen peroxide to brominate electrophilic organics.
Murex snails have a bromoperoxidase used to produce Tyrian purple dye. The enzyme is very specific to bromide and physically stable, but has not been characterized as to its active site.
| Haloperoxidase | Oxidisable halide | Origin, Notes |
| Chloroperoxidase | Cl−, Br−, I− | neutrophils, eosinophils Caldariomyces fumago |
| Bromoperoxidase | Br−, I− | milk, saliva, tears, sea urchin eggs, vanadium bromoperoxidase,, Murex snail bromoperoxidase |
| Iodoperoxidase | I− | horseradish thyroid |