NADPH-dependent covalent binding of [3H]paroxetine to human liver microsomes and S-9 fractions: identification of an electrophilic quinone metabolite of paroxetine.

@article{Zhao2007NADPHdependentCB,
  title={NADPH-dependent covalent binding of [3H]paroxetine to human liver microsomes and S-9 fractions: identification of an electrophilic quinone metabolite of paroxetine.},
  author={Sabrina X Zhao and Deepak K. Dalvie and Joan M Kelly and John R Soglia and Kosea S Frederick and Evan B Smith and R Scott Obach and Amit S Kalgutkar},
  journal={Chemical research in toxicology},
  year={2007},
  volume={20 11},
  pages={1649-57}
}
The primary pathway of clearance of the methylenedioxyphenyl-containing compound and selective serotonin reuptake inhibitor paroxetine in humans involves P450 2D6-mediated demethylenation to a catechol intermediate. The process of demethylenation also results in the mechanism-based inactivation of the P450 isozyme. While the link between P450 2D6 inactivation and pharmacokinetic interactions of paroxetine with P450 2D6 substrates has been firmly established, there is a disconnect in terms of… CONTINUE READING
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