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Hydroperoxide-dependent sulfoxidation catalyzed by soybean microsomes.

E Blee, F Durst

    Archives of Biochemistry and Biophysics
    |April 1, 1987
    PubMed
    Summary

    Soybean microsomes catalyze methiocarb sulfoxidation using hydroperoxides, not molecular oxygen. This process, independent of NAD(P)H, highlights a novel hydroperoxide-dependent S-oxidation pathway.

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    Area of Science:

    • Biochemistry
    • Environmental Science
    • Plant Science

    Background:

    • Methiocarb is an aromatic-alkyl sulfide pesticide.
    • Sulfoxidation is a key metabolic pathway for pesticides.
    • Soybean microsomes are commonly used in plant-based detoxification studies.

    Purpose of the Study:

    • To investigate the mechanism of methiocarb sulfoxidation catalyzed by soybean microsomes.
    • To determine the role of hydroperoxides in this S-oxidation reaction.
    • To identify the enzyme responsible for methiocarb sulfoxidation.

    Main Methods:

    • Sulfoxidation assays using methiocarb as substrate.
    • 18O2-labeling experiments to trace oxygen origin.
    • Enzyme activity measurements in the presence and absence of cofactors and exogenous hydroperoxides.

    Main Results:

    • Methiocarb sulfoxidation was significantly enhanced by cumene and linoleic acid hydroperoxides.
    • The reaction is hydroperoxide-dependent, with oxygen originating from hydroperoxides, not molecular oxygen.
    • Basal sulfoxidation occurred due to endogenous hydroperoxides, particularly those from free fatty acids.
    • Cytochrome P-450 was ruled out; the enzyme showed similarities to plant peroxygenase.

    Conclusions:

    • Soybean microsomes catalyze a novel hydroperoxide-dependent S-oxidation of methiocarb.
    • The enzyme involved is likely a plant peroxygenase, not cytochrome P-450.
    • This pathway is significant for understanding pesticide metabolism in plants.

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