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

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

Standard

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, 2011, p. 132-138.

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

Harvard

Laursen, T, Jensen, K & Møller, BL 2011, 'Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450', Biochimica et Biophysica Acta - Proteins and Proteomics, vol. 1814, no. 1, pp. 132-138. https://doi.org/10.1016/j.bbapap.2010.07.003

APA

Laursen, T., Jensen, K., & Møller, B. L. (2011). Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450. Biochimica et Biophysica Acta - Proteins and Proteomics, 1814(1), 132-138. https://doi.org/10.1016/j.bbapap.2010.07.003

Vancouver

Laursen T, Jensen K, Møller BL. Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450. Biochimica et Biophysica Acta - Proteins and Proteomics. 2011;1814(1):132-138. https://doi.org/10.1016/j.bbapap.2010.07.003

Author

Laursen, Tomas ; Jensen, Kenneth ; Møller, Birger Lindberg. / Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450. In: Biochimica et Biophysica Acta - Proteins and Proteomics. 2011 ; Vol. 1814, No. 1. pp. 132-138.

Bibtex

@article{608dd29a5a9f47d38109d3d61ad6fc43,
title = "Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450",
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{"}.",
author = "Tomas Laursen and Kenneth Jensen and M{\o}ller, {Birger Lindberg}",
note = "Cytochrome P450: Structure, biodiversity and potential for application ",
year = "2011",
doi = "10.1016/j.bbapap.2010.07.003",
language = "English",
volume = "1814",
pages = "132--138",
journal = "B B A - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450

AU - Laursen, Tomas

AU - Jensen, Kenneth

AU - Møller, Birger Lindberg

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

PY - 2011

Y1 - 2011

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".

U2 - 10.1016/j.bbapap.2010.07.003

DO - 10.1016/j.bbapap.2010.07.003

M3 - Journal article

C2 - 20624491

VL - 1814

SP - 132

EP - 138

JO - B B A - Proteins and Proteomics

JF - B B A - Proteins and Proteomics

SN - 1570-9639

IS - 1

ER -

ID: 32167860