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Todd D. Porter, Ph.D.


NADPH-cytochrome P450 reductase (CPR) is the electron donor protein for several oxygenase enzymes found on the endoplasmic reticulum of most eukaryotic cells.  These oxygenases include the cytochromes P450, a family of enzymes involved in the metabolism of many drugs and dietary substances, and in the synthesis of steroid hormones and other extracellular lipid signaling molecules; heme oxygenase, a hemeprotein that catalyzes the first step in the degradation of heme to bilirubin; and squalene monooxygenase, the second enzyme in the committed pathway for sterol biosynthesis.  CPR may also donate electrons to 7-dehydrocholesterol reductase in the sterol synthesis pathway, and to cytochrome b5, which supports both sterol synthesis and the fatty acid desaturase and elongase pathways.

Cytochrome P450 reductase redox partners


CPR structural cartoon


CPR is a flavoprotein containing both FAD and FMN.  It has a modular structure suggestive of its evolution from smaller subunits similar to flavodoxins and ferredoxin NADP+ reductase, and its 3-dimensional structure was recently determined.  CPR is also a component of nitric oxide synthases and methionine synthase reductase.  My laboratory is carrying out structural studies on this unique flavoprotein through site-directed mutagenesis, with the goal of generating biotechnological applications for this versatile reductase.


Further Information on Cytochrome P450 Reductase



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David Nelson's P450 Web Matrix

Comments to Todd D. Porter, Pharmaceutical Sciences, University of Kentucky College of Pharmacy, Lexington, KY 40536-0082.  Phone 859 257-1137; FAX 859 257-7564
Last Modified: September 27, 2001
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