NADPH-Dependent Cytochrome P450 Reductase

  • Anthony Y. H. Lu
Part of the NATO ASI Series Advanced Science Institutes Series book series (NSSA, volume 202)


The pioneering studies of Horecker (1), Phillips and Langdon (2), Williams and Kamin (3) established that the microsomal NADPH-cytochrome c reductase is a flavoprotein capable of reducing various electron acceptors. Subsequent studies by other investigators (4–6) suggested an involvement of this reductase in microsomal hydroxylation since like cytochrome P450, it is inducible by phenobarbital. In addition, microsomal monooxygenase activity can be inhibited by cytochrome c (7) and antibodies against the reductase (8–10). A direct involvement of this enzyme in hydroxylation was established when the liver microsomal monooxygenase system was solubilized, resolved and reconstituted (11, 12). In these studies, the flavoprotein was shown to be an obligatory component in hydroxylation, transferring reducing equivalents from NADPH to cytochrome P450. Since then, the term NADPH-cytochrome P450 reductase has been used to reflect its physiological function.


Dynamic Nuclear Polarization P450 Reductase Phospholipid Vesicle Cytochrome P450 Reductase Hydrophilic Domain 
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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Anthony Y. H. Lu
    • 1
  1. 1.Merck Sharp & Dohme Research LaboratoriesRahwayUSA

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