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

Tomas Laursen; Kenneth Jensen; Birger Lindberg Møller

doi:10.1016/j.bbapap.2010.07.003

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

Tomas Laursen, Kenneth Jensen, Birger Lindberg Møller

78 Citations (Scopus)

Abstract

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".

Original language	English
Journal	Biochimica et Biophysica Acta - Proteins and Proteomics
Volume	1814
Issue number	1
Pages (from-to)	132-138
Number of pages	7
ISSN	1570-9639
DOIs	https://doi.org/10.1016/j.bbapap.2010.07.003
Publication status	Published - Jan 2011

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Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450. / Laursen, Tomas; Jensen, Kenneth; Møller, Birger Lindberg.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1814, No. 1, 01.2011, p. 132-138.

Research output: Contribution to journal › Journal article › Research › peer-review

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N1 - Cytochrome P450: Structure, biodiversity and potential for application

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N2 - 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".

AB - 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".

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

Abstract

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