Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3.

@article{Kitazume2007ObligatoryIE,
  title={Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3.},
  author={Tatsuya Kitazume and Donovan C. Haines and Ronald W. Estabrook and Baozhi Chen and Julian Peterson},
  journal={Biochemistry},
  year={2007},
  volume={46 42},
  pages={11892-901}
}
Cytochromes P450 typically catalyze the monooxygenation of hydrophobic compounds resulting in the insertion of one atom of dioxygen into the organic substrate and the reduction of the other oxygen atom to water. The two electrons required for the reaction are normally provided by another redox active protein, for example cytochrome P450 reductase (CPR) in mammalian endoplasmic reticulum membranes. P450BM-3 from Bacillus megaterium is a widely studied P450 cytochrome in which the P450 is fused… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 16 extracted citations

Similar Papers

Loading similar papers…