Haloperoxidase
Haloperoxidases are
Mechanistic and thermodynamic considerations
Halogenations of organic compounds by free halogens (F2, Cl2, Br2, and sometimes I2) is generally favorable process. It is practiced industrially on a large scale for example. In nature, however, free halogens do not exist in appreciable amounts. The combination of hydrogen peroxide, which is widely produced by aerobic life, and halide anionsCl−, Br−, I− provides the equivalent of Cl2, Br2, I2. The oxidation of these anions by hydrogen peroxide is slow in the absence of enzymes. These enzymes are called haloperoxidases. The reaction that they catalyze is:
- X− + H2O2 + H+ + R−H → X + 2 H2O + R−X
From the perspective of thermodynamics, the
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.[3]
The mammalian haloperoxidases
A specific vanadium bromoperoxidase in marine organisms (fungi, bacteria, microalgae, perhaps other eukaryotes) uses vanadate and hydrogen peroxide to brominate electrophilic organics.[5]
Haloperoxidase | Oxidisable halide | Origin, Notes |
---|---|---|
Chloroperoxidase (CPO) | Cl−, Br−, I− | neutrophils (myeloperoxidase), eosinophils (eosinophil peroxidase, can use Cl−, prefers Br−) |
Bromoperoxidase (BPO)
|
Br−, I− | milk, saliva, tears (lactoperoxidase), sea urchin eggs (ovoperoxidase), |
Iodoperoxidase (IPO)
|
I− | horseradish (horseradish peroxidase) |
See also
References
- ISBN 0-85312-984-3
- PMID 16895332.
- ^ [1] Archived 2009-05-26 at the Wayback Machine Eosinophils preferentially use bromide to generate halogenating agents - Mayeno et al. 264 (10): 5660 - Journal of Biological Chemistry
- ^ [2] Role of Heme-Protein Covalent Bonds in Mammalian Peroxidases
- PMID 19363038.