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Koymans; T. Kamataki; J. J. Stegeman; R. Feyereisen; D. J. Waxman; M. R. Waterman; Ο. Gotoh; M. J. Coon; R. W. Estabrook; I. C. Gunsalus, D. W. Nebert; Pharmacogenetics 1996, 6, 1-42. D. R. html 1998. C. elegans. Consortium; Science 1998, 282, 2012-2018. M. D. Adams; S. E. Celniker; R. A. Holt; C. A. Evans; J. D. ; Science 2000, 287, 2185-2195. R. L. P. Lindberg, M. Negishi; Nature 1989, 339, 632-634. M. Agosin, In Comprehensive Insect Physiology, Biochemistry, and Pharmacology; Kerkut, G. A. and Gilbert, L.

Cytochrome P450 (P450) is a hemoprotein which acts as the terminal oxidase in monooxygenase systems and there are multiple P450s in eukaryotic species. Monooxygenases are remarkable in that they can oxidize widely diverse substrates and are capable of producing a bewildering array of reactions (1-3). Monooxygenase-mediated oxidation requires (besides oxygen and substrate) P450, NADPH cytochrome P450 oxidoreductase (P450 reductase), NADPH and phospholipid (4). P450 reductase is required to transfer reducing equivalents from NADPH to P450.

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