Biodehalogenation: reactions of cytochrome P-450 with polyhalomethanes.

@article{Castro1985BiodehalogenationRO,
  title={Biodehalogenation: reactions of cytochrome P-450 with polyhalomethanes.},
  author={Charles E. Castro and Ruth S. Wade and N. O. Belser},
  journal={Biochemistry},
  year={1985},
  volume={24 1},
  pages={204-10}
}
The products, stoichiometry, and kinetics of the oxidation of the enzyme cytochrome P-450 cam by five polyhalomethanes and chloronitromethane are described. The reactivity of the enzyme is compared with that of deuteroheme and with the enzyme in its native cell, Pseudomonas putida (PpG-786). In all cases, the reaction entails hydrogenolysis of the carbon-halogen bond: 2FeIIP + RCXn----2FeIIIP + RCHXn-1 (P = porphyrin or P-450 cam in vitro and in vivo). Trichloronitromethane was the fastest… CONTINUE READING

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