Haloperoxidase
Haloperoxidases are peroxidases that are able to mediate the oxidation of halides by hydrogen peroxide.[1][2] Both halides and hydrogen peroxide are widely available in the environment.
The Nernst equation shows that hydrogen peroxide can oxidize chloride (E°= 1.36 V), bromide (E°= 1.09 V) and iodide (E°= 0.536 V) from a thermodynamic perspective under natural conditions, i.e., a temperature range of about 0–30 °C and a pH ranging from about 3 (humic soil layer) to about 8 (sea water). Fluoride (E°= 2.87 V) 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.[3]
The mammalian haloperoxidases myeloperoxidase (MPO), lactoperoxidase (LPO) and eosinophil peroxidase (EPO) are also capable of oxidizing the pseudohalide thiocyanate (SCN−). 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.[4]
A specific vanadium bromoperoxidase in marine organisms (fungi, bacteria, microalgae, perhaps other eukaryotes) uses vanadate and hydrogen peroxide to brominate electrophilic organics.[5]
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 (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
- ^ S.L. Neidleman, J. Geigert (1986) Biohalogenation - principles, basic roles and applications; Ellis Horwood Ltd Publishers; Chichester; ISBN 0-85312-984-3
- ^ Menon, Binuraj R. K.; Richmond, Daniel; Menon, Navya (2020-10-15). "Halogenases for biosynthetic pathway engineering: Toward new routes to naturals and non-naturals". Catalysis Reviews: 1–59. doi:10.1080/01614940.2020.1823788. ISSN 0161-4940.
- ^ [1] 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
- ^ Winter, JM; Moore, BS (July 2009). "Exploring the chemistry and biology of vanadium-dependent haloperoxidases". J. Biol. Chem. 284: 18577–81. doi:10.1074/jbc.R109.001602. PMC 2707250. PMID 19363038.
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