Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1814, Issue 1, Pages 132-138Publisher
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
Categories
Funding
- Danish Council on Technology and Production Sciences
- Villum Kann Rasmussen Foundation
- Danish Ministry of Science, Technology and Innovation
- Faculty of Life Sciences, University of Copenhagen
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available