Mechanism of the acyl-carbon cleavage and related reactions catalyzed by multifunctional P-450s: studies on cytochrome P-450(17)alpha.

@article{Akhtar1994MechanismOT,
  title={Mechanism of the acyl-carbon cleavage and related reactions catalyzed by multifunctional P-450s: studies on cytochrome P-450(17)alpha.},
  author={Muhammad Akhtar and David P. Corina and Stephan K Miller and A Z Shyadehi and J Neville Wright},
  journal={Biochemistry},
  year={1994},
  volume={33 14},
  pages={4410-8}
}
It is now well-known that conventional cytochrome P-450s catalyze hydroxylation reactions using an iron mono-oxygen species, the structure of which, as inferred from chemical model studies, may be drrepresented by the following canonical forms: FeV==O<-->(.+)FeIV==O<-->FeIV--O(.). Certain multifunctional P-450s, notably those involved in steroid biosynthesis, catalyze, in addition to hydroxylation reactions, an acyl-carbon cleavage process in which the participation of an iron peroxide… CONTINUE READING

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