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Lipid-exchange in nanodiscs discloses membrane boundaries of cytochrome-P450 reductase.


ABSTRACT: Lipids are critical for the function of membrane proteins. NADPH-cytochrome-P450-reductase, the sole electron transferase for microsomal oxygenases, possesses a conformational dynamics entwined with its topology. Here, we use peptide-nanodiscs to unveil cytochrome-P450-reductase's lipid boundaries, demonstrating a protein-driven enrichment of ethanolamine lipids (by 25%) which ameliorates by 3-fold CPR's electron-transfer ability.

SUBMITTER: Barnaba C 

PROVIDER: S-EPMC6022741 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

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Lipid-exchange in nanodiscs discloses membrane boundaries of cytochrome-P450 reductase.

Barnaba Carlo C   Ravula Thirupathi T   Medina-Meza Ilce G IG   Im Sang-Choul SC   Anantharamaiah G M GM   Waskell Lucy L   Ramamoorthy Ayyalusamy A  

Chemical communications (Cambridge, England) 20180601 49


Lipids are critical for the function of membrane proteins. NADPH-cytochrome-P450-reductase, the sole electron transferase for microsomal oxygenases, possesses a conformational dynamics entwined with its topology. Here, we use peptide-nanodiscs to unveil cytochrome-P450-reductase's lipid boundaries, demonstrating a protein-driven enrichment of ethanolamine lipids (by 25%) which ameliorates by 3-fold CPR's electron-transfer ability. ...[more]

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