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

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 underg...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2011, Vol.1814 (1), p.132-138
Main Authors: Laursen, Tomas, Jensen, Kenneth, Møller, Birger Lindberg
Format: Article
Language:English
Subjects:
Animals
Cytochrome P-450 Enzyme System - chemistry
Cytochrome P-450 Enzyme System - metabolism
Electron Transport
Flavins - chemistry
Flavins - metabolism
FMN-binding domain
Models, Molecular
NADPH-cytochrome P450 oxidoreductase
NADPH-Ferrihemoprotein Reductase - chemistry
NADPH-Ferrihemoprotein Reductase - metabolism
Nitric oxide synthase
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Rats
Rotating model
Swinging model
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Summary: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”.
ISSN:1570-9639
0006-3002
1878-1454
DOI:10.1016/j.bbapap.2010.07.003