Peripheral ligand-binding site in cytochrome P450 3A4 located with fluorescence resonance energy transfer (FRET).

@article{Davydov2012PeripheralLS,
  title={Peripheral ligand-binding site in cytochrome P450 3A4 located with fluorescence resonance energy transfer (FRET).},
  author={D. R. Davydov and Jessica A. O. Rumfeldt and Elena V. Sineva and H. K. D. H. Fernando and Nadezhda Y Davydova and James R. Halpert},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 9},
  pages={6797-809}
}
The mechanisms of ligand binding and allostery in the major human drug-metabolizing enzyme cytochrome P450 3A4 (CYP3A4) were explored with fluorescence resonance energy transfer (FRET) using a laser dye, fluorol-7GA (F7GA), as a model substrate. Incorporation into the enzyme of a thiol-reactive FRET probe, pyrene iodoacetamide, allowed us to monitor the binding by FRET from the pyrene donor to the F7GA acceptor. Cooperativity of the interactions detected by FRET indicates that the enzyme… CONTINUE READING
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