Activation of 4-nitro-o-phenylenediamine by the S2 fraction of Zea mays to mutagenic product(s)

Studies on plant metabolic activation with the S2 fraction from Zea mays have been developed. The 4-nitro-o-phenylenediamine (NOP) activation by S2 has been analyzed with the Ames test as a short-term assay. The NOP mutagenic potency was increased two-fold by S2, while rat liver S9 produced the contrary effect. The presence of a NADPH-generating system and the treatment of S2 with CO do not modify S2 activation of NOP. In this fraction, neither cytochrome P450 nor some enzymatic activities depending on cyt-P450 (aniline hydroxylase and aminopyrine demethylase) were detected. Therefore, the enhancement of NOP mutagenic potency by S2 is independent of the mixed-function oxidase system. On the other hand, inhibitors of the peroxidase activity such as N-acetyl-p-aminophenol caused a partial inhibition of S2 activation of NOP. Likewise, diethyldithiocarbamate produced both a reduction of the S2 peroxidase activity in biochemical assays and a partial inhibition of S2 activation of NOP. Moreover, it was possible to find a direct correlation between the activity of peroxidase per plate of both the S2 fraction and horseradish peroxidase and the number of revertants induced by NOP in the TA98 strain. On the basis of these results, we report that a HRP-like peroxidase activity must be the main pathway of NOP activation by the plant metabolic activation system studied in this work. © 1994.