An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase

Mukherjee, Nandekar and Wade investigate the structural arrangement of the complex between membrane-bound cytochrome P450 1A1 and NADPH-cytochrome P450 reductase. They find that upon binding to the reductase, the catalytic domain of cytochrome P450 1A1 reorients subject to the constraints of membran...

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Autores principales: Goutam Mukherjee, Prajwal P. Nandekar, Rebecca C. Wade
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/b6c55376663c4ca48528fe879b9a75a4
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spelling oai:doaj.org-article:b6c55376663c4ca48528fe879b9a75a42021-12-02T15:07:32ZAn electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase10.1038/s42003-020-01568-y2399-3642https://doaj.org/article/b6c55376663c4ca48528fe879b9a75a42021-01-01T00:00:00Zhttps://doi.org/10.1038/s42003-020-01568-yhttps://doaj.org/toc/2399-3642Mukherjee, Nandekar and Wade investigate the structural arrangement of the complex between membrane-bound cytochrome P450 1A1 and NADPH-cytochrome P450 reductase. They find that upon binding to the reductase, the catalytic domain of cytochrome P450 1A1 reorients subject to the constraints of membrane binding, potentially explaining why the electron transfer rates between the proteins are low when compared to those of soluble bacterial cytochrome P450s.Goutam MukherjeePrajwal P. NandekarRebecca C. WadeNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-13 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Goutam Mukherjee
Prajwal P. Nandekar
Rebecca C. Wade
An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase
description Mukherjee, Nandekar and Wade investigate the structural arrangement of the complex between membrane-bound cytochrome P450 1A1 and NADPH-cytochrome P450 reductase. They find that upon binding to the reductase, the catalytic domain of cytochrome P450 1A1 reorients subject to the constraints of membrane binding, potentially explaining why the electron transfer rates between the proteins are low when compared to those of soluble bacterial cytochrome P450s.
format article
author Goutam Mukherjee
Prajwal P. Nandekar
Rebecca C. Wade
author_facet Goutam Mukherjee
Prajwal P. Nandekar
Rebecca C. Wade
author_sort Goutam Mukherjee
title An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase
title_short An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase
title_full An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase
title_fullStr An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase
title_full_unstemmed An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase
title_sort electron transfer competent structural ensemble of membrane-bound cytochrome p450 1a1 and cytochrome p450 oxidoreductase
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/b6c55376663c4ca48528fe879b9a75a4
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