Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.

@article{Sugishima2014StructuralBF,
  title={Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.},
  author={Masakazu Sugishima and Hideaki Sato and Yuichiro Higashimoto and Jiro Harada and Kei Wada and Keiichi Fukuyama and Masato Noguchi},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 7},
  pages={2524-9}
}
NADPH-cytochrome P450 oxidoreductase (CPR) supplies electrons to various heme proteins including heme oxygenase (HO), which is a key enzyme for heme degradation. Electrons from NADPH flow first to flavin adenine dinucleotide, then to flavin mononucleotide (FMN), and finally to heme in the redox partner. For electron transfer from CPR to its redox partner, the ''closed-open transition'' of CPR is indispensable. Here, we demonstrate that a hinge-shortened CPR variant, which favors an open… CONTINUE READING
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Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450

  • D Hamdane
  • J Biol Chem 284(17):11374–11384
  • 2009

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