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Related Experiment Videos

Halohydrocarbon synthesis by bromoperoxidase.

R Theiler, J C Cook, L P Hager

    Science (New York, N.Y.)
    |December 8, 1978
    PubMed
    Summary
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    Marine red algae enzyme bromoperoxidase incorporates bromine into organic substrates. This enzyme produces volatile brominated hydrocarbons, suggesting a role in natural halogenation processes.

    Area of Science:

    • Marine biology
    • Biochemistry
    • Enzymology

    Background:

    • Marine organisms produce halometabolites.
    • Bromoperoxidases are enzymes involved in halogenation.

    Purpose of the Study:

    • To investigate the enzymatic activity of bromoperoxidase from Bonnemaisonia hamifera.
    • To identify brominated compounds produced by the enzyme.

    Main Methods:

    • Extraction and partial purification of bromoperoxidase from marine red algae.
    • Enzymatic assays using hydrogen peroxide, bromide ion, and 3-oxooctanoic acid.
    • Analysis of volatile brominated hydrocarbons using gas chromatography-mass spectrometry.

    Main Results:

    • The bromoperoxidase incorporated bromine into 3-oxooctanoic acid.

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  • Formation of dibromomethane, bromoform, and 1-pentyl bromide was observed.
  • Enzyme activity was optimal in the pH range of 5 to 8.

    • Conclusions:

    • Bromoperoxidase from Bonnemaisonia hamifera catalyzes the formation of volatile halohydrocarbons.
    • Enzymatic halogenation by bromoperoxidases may contribute to natural halometabolite production in marine environments.