The biochemical mechanisms of the plant activation of promutagenic aromatic amines

Elizabeth D. Wagner, Mary M. Verdier, Michael J. Plewa

Research output: Contribution to journalArticlepeer-review


Using specific monooxygenase and oxidase inhibitors in a plant cell/microbe coincubation assay, the biochemical mechanisms of the plant activation of two aromatic amines were compared. The biological endpoints included mutation induction, inhibition of mutagenicity, viability of the plant cells (activating system), and viability of the microbial cells (genetic indicator organism). The activation of m‐phenylenediamine by TX1 cells was mediated by enzyme systems that were inhibited by diethyldithiocarbamate, potassium cyanide, methimazole, ( + )‐catechin or acetaminophen. The inhibition by metyrapone was attended by toxicity in the plant cells. These data implicate a TX1 cell peroxidase and a FAD‐dependent monooxygenase in the plant activation of m‐phenylenediamine. The TX1 cell activation of 2‐aminofluorene was inhibited by diethyldithiocarbamate, 7,8‐benzoflavone, acetaminophen or ( + )‐catechin. An additional pathway of the plant cells in the activation of 2‐aminofluorene may involve a cytochrome P‐448‐type N‐hydroxylase.

Original languageEnglish (US)
Pages (from-to)236-244
Number of pages9
JournalEnvironmental and Molecular Mutagenesis
Issue number4
StatePublished - 1990


  • 2‐aminofluorene
  • antimutagenesis
  • monooxygenase
  • m‐phenylenediamine
  • oxidase inhibitors

ASJC Scopus subject areas

  • Epidemiology
  • Genetics(clinical)
  • Health, Toxicology and Mutagenesis


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