Effects of specific monooxygenase and oxidase inhibitors on the activation of 2-aminofluorene by plant cells

Elizabeth D. Wagner, James M. Gentile, Michael Jacob Plewa

Research output: Contribution to journalArticle

Abstract

Using specific inhibitors, a plant cell/microbe coincubation assay was employed to investigate biochemical mechanisms of plant activation. The biological endpoints of mutation induction, inhibition of mutagenicity and viability of the plant-activating system as well as viability of the microbiological indicator were simultaneously assayed from the same reaction tube. We investigated six inhibitors of monooxygenases and oxidases (diethyldithiocarbamate, methimazole, metyrapone, (+)-catechin, 7,8-benzoflavone and potassium cyanide). The activation of 2-aminofluorene by TX1 cells was mediated by an enzyme systems(s) that was inhibited by μM amounts of diethyldithiocarbamate or 7,8-benzoflavone. (+)-Catechin (at low concentrations) or methimazole enhanced the activation of 2-aminofluorene while higher concentrations of (+)-catechin were inhibitory. These data indicate that a significant pathway of the plant activation of 2-aminofluorene is via a cytochrome P-448-type N-hydroxylase. The presence of a FAD-dependent monooxygenase was not detected.

Original languageEnglish (US)
Pages (from-to)163-178
Number of pages16
JournalMutation Research/Environmental Mutagenesis and Related Subjects
Volume216
Issue number3
DOIs
StatePublished - Jun 1989

Keywords

  • 2-Aminofluorene
  • Monooxygenase inhibitor
  • Oxidase inhibitor
  • Plant activation, mechanisms

ASJC Scopus subject areas

  • Toxicology
  • Genetics

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