Complex reactions catalyzed by cytochrome P450 enzymes.

Isin EM, Guengerich FP
Biochim Biophys Acta. 2007 1770 (3): 314-29

PMID: 17239540 · DOI:10.1016/j.bbagen.2006.07.003

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.

MeSH Terms (9)

Animals Catalysis Cytochrome P-450 Enzyme System Dimerization Humans Hydroxylation Mixed Function Oxygenases Oxidation-Reduction Substrate Specificity

Connections (1)

This publication is referenced by other Labnodes entities: