Haloperoxidase

Source: Wikipedia, the free encyclopedia.

Haloperoxidases are

environment.[2]

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

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

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]

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)
Caldariomyces fumago

Bromoperoxidase
(BPO)
Br, I milk, saliva, tears (lactoperoxidase),

sea urchin eggs (ovoperoxidase),
vanadium bromoperoxidase,(marine algae, other marine spp.?),
Murex snail bromoperoxidase (does not use I or Cl)

Iodoperoxidase
(IPO)
I horseradish (horseradish peroxidase)

thyroid (thyroid peroxidase)

See also

References

  1. .
  2. ^ [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
  3. ^ [2] Role of Heme-Protein Covalent Bonds in Mammalian Peroxidases
  4. PMID 19363038
    .