NADPH Cytochrome P450 Reductase and Its Structural and Functional Domains

  • Henry W. Strobel
  • Anne V. Hodgson
  • Sijiu Shen


NADPH cytochrome P450 reductase has been a topic of interest and study since Horecker1 first reported the isolation from pig liver after acetone extraction and trypsin treatment of a protein that catalyzed the reduction of cytochromes c. Since that initial report, much information has been revealed and reported about the nature, reactivities, structure, and regulation of the reductase that we have come to recognize as a component of the cytochrome P450-dependent drug metabolism system. The development of knowledge about the role and mechanism of NADPH cytochrome P450 reductase has been periodically discussed and reviewed.2–5 The most recent review (by Backes5) in 1993 focused on the function of cytochrome P450 reductase, summarizing and evaluating very elegantly a number of studies of the mechanism of electron transfer to the flavin centers of the reductase, interflavin electron transfer and transfer of electrons from the flavin centers to oxygen and/or the redox partners of cytochrome P450 reductase. This present review, therefore, will not cover mechanism in any more than a cursory fashion, but will attempt to focus on a summary of the salient features of the study of structural/functional regions or domains of cytochrome P450 reductase.


P450 Reductase Cytochrome P450 Reductase Redox Partner NADPH Cytochrome P450 Reductase Antipeptide Antibody 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Henry W. Strobel
    • 1
  • Anne V. Hodgson
    • 1
  • Sijiu Shen
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyThe University of Texas Medical School at HoustonHoustonUSA

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