Complex reactions catalyzed by cytochrome P450 enzymes

Biochim Biophys Acta. 2007 Mar;1770(3):314-29. doi: 10.1016/j.bbagen.2006.07.003. Epub 2006 Jul 13.


Cytochrome P450 (P450) enzymes are some of the most versatile redox proteins known. The basic P450 reactions include C-hydroxylation, heteroatom oxygenation, heteroatom release (dealkylation), and epoxide formation. Mechanistic explanations for these reactions have been advanced. A number of more complex P450 reactions also occur, and these can be understood largely in the context of the basic chemical mechanisms and subsequent rearrangements. The list discussed here updates a 2001 review and includes chlorine oxygenation, aromatic dehalogenation, formation of diindole products, dimer formation via Diels-Alder reactions of products, ring coupling and also ring formation, reductive activation (e.g., aristolochic acid), ring contraction (piperidine nitroxide radical), oxidation of troglitazone, cleavage of amino oxazoles and a 1,2,4-oxadiazole ring, bioactivation of a dihydrobenzoxathiin, and oxidative aryl migration.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Catalysis
  • Cytochrome P-450 Enzyme System / chemistry
  • Cytochrome P-450 Enzyme System / metabolism*
  • Dimerization
  • Humans
  • Hydroxylation
  • Mixed Function Oxygenases / metabolism
  • Oxidation-Reduction
  • Substrate Specificity


  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases