HORSERADISH PEROXIDASE-HYDROGEN PEROXIDE-CATALYZED OXIDATION OF CARCINOGEN N-HYDROXY-N-ACETYL-2-AMINOFLUORENE AS EFFECTED BY CYANIDE AND ASCORBATE

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  • 1 January 1976
    • journal article
    • research article
    • Vol. 36  (4) , 1510-1519
Abstract
Horseradish peroxidase and H2O2 mediate N-hydroxy-N-acetyl-2-aminofluorene (N-OH-AAF) conversion into 2 more potent carcinogens, 2-nitrosofluorene and N-acetoxy-N-acetyl-2-aminofluorene. Optical studies of this system indicate that horseradish peroxidase is operating as a peroxidase with N-OH-AFF as the electron donor. 2-nitrosofluorene and N-acetoxy-N-acetyl-2-aminofluorene apparently are the products of the type II enzyme-mediated oxidation of N-OH-AAF, but the results with the type VI enzyme indicate that more 2-nitrosofluorene was formed and, in addition, another product absorbing at 245 nm was formed. If ascorbate is present in the N-OH-AAF/horseradish peroxidase/H2O2 system, ascorbate is oxidized preferentially. Cyanide, a known inhibitor of the peroxidase, does not inhibit when N-OH-AAF is the electron donor. The reaction products are the same in the presence or absence of cyanide.

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