Targeting of the highly conserved threonine 302 residue of cytochromes P450 2B family during mechanism-based inactivation by aryl acetylenes.

@article{Zhang2011TargetingOT,
  title={Targeting of the highly conserved threonine 302 residue of cytochromes P450 2B family during mechanism-based inactivation by aryl acetylenes.},
  author={Haoming Zhang and Hsia-lien Lin and Cesar Kenaan and Paul F. Hollenberg},
  journal={Archives of biochemistry and biophysics},
  year={2011},
  volume={507 1},
  pages={135-43}
}
Cytochromes P450 (CYPs or P450s) contain a highly conserved threonine residue in the active site, which is referred to as Thr302 in the amino acid sequence of CYP2B4. Extensive biochemical and crystallographic studies have established that this Thr302 plays a critical role in activating molecular oxygen to generate Compound I, a putative iron(IV)-oxo porphyrin cation radical, that carries out the preliminary oxygenation of CYP substrates. Because of its proximity to the center of the P450… CONTINUE READING