Identification of the Binding Site on Cytochrome P450 2B4 for Cytochrome b 5 and Cytochrome P450 Reductase*

@article{Bridges1998IdentificationOT,
  title={Identification of the Binding Site on Cytochrome P450 2B4 for Cytochrome b 5 and Cytochrome P450 Reductase*},
  author={A. Bridges and L. Gruenke and Y. T. Chang and I. Vakser and G. Loew and L. Waskell},
  journal={The Journal of Biological Chemistry},
  year={1998},
  volume={273},
  pages={17036 - 17049}
}
A model of cytochrome P450 2B4, which was constructed by homology modeling with the four known crystal structures of the cytochromes P450 (Chang, T.-T., Stiffelman, O. B., Vakser, I. A., Loew, G. H., Bridges, A., and Waskell, L. (1997)Protein Eng. 10, 119–129), was used to select amino acids predicted, by computer docking studies and numerous previous biochemical and site-directed mutagenesis studies, to be involved in binding the heme domain of cytochrome b 5. Twenty-four amino acid residues… Expand
An open conformation of mammalian cytochrome P450 2B4 at 1.6-Å resolution
  • E. E. Scott, Y. He, +5 authors C. Stout
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2003
Mapping of interaction between cytochrome P450 2B4 and cytochrome b5: the first evidence of two mutual orientations.
Overexpression and purification of the membrane-bound cytochrome P450 2B4.
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