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Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450

Journal

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2010.07.003

Keywords

NADPH-cytochrome P450 oxidoreductase; FMN-binding domain; Swinging model; Rotating model; Nitric oxide synthase

Funding

  1. Danish Council on Technology and Production Sciences
  2. Villum Kann Rasmussen Foundation
  3. Danish Ministry of Science, Technology and Innovation
  4. Faculty of Life Sciences, University of Copenhagen

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The NADPH-dependent cytochrome P450 reductase (CPR) is a key electron donor to eucaryotic cytochromes P450 (CYPs). CPR shuttles electrons from NADPH through the FAD and FMN-coenzymes into the iron of the prosthetic heme-group of the CYP. In the course of these electron transfer reactions, CPR undergoes large conformational changes. This mini-review discusses the new evidence provided for such conformational changes involving a combination of a swinging and rotating model and highlights the molecular mechanisms by which formation of these conformations are controlled and thereby enables CPR to serve as an effective electron transferring nano-machine. (C) 2010 Elsevier B.V. All rights reserved.

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