Hydroxylation of primisulfuron by an inducible cytochrome P450-dependent monooxygenase system from maize

@article{FonnPfister1990HydroxylationOP,
  title={Hydroxylation of primisulfuron by an inducible cytochrome P450-dependent monooxygenase system from maize},
  author={R. Fonn{\'e}-Pfister and J. Gaudin and K. Kreuz and K. Ramsteiner and E. Ebert},
  journal={Pesticide Biochemistry and Physiology},
  year={1990},
  volume={37},
  pages={165-173}
}
Abstract Microsomes were prepared from etiolated maize seedlings and incubated with [14C]primisulfuron (2-[3-(4,6-bis(difluoromethoxy)-pyrimidin-2-yl)-ureidosulfonyl]-benzoic acid methylester). Two enzymatic reaction products were formed in the presence of O2 and NADPH. Comparison on high-performance liquid chromatography with synthetic reference standards and mass spectrometry of the two in vitro metabolites revealed that [14C]primisulfuron was hydroxylated at two different sites, i.e., at the… Expand
Multiple forms of plant cytochromes p-450.
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