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Detergent-free isolation of CYP450-reductase's FMN-binding domain in E. coli lipid-nanodiscs using a charge-free polymer.

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The membrane-anchored flavin mononucleotide binding domain (FBD) of CYP450 reductase was extracted in E. coli lipid-nanodiscs using charge-free pentyl-inulin polymer. FBD in nanodiscs was found to be conformationally homogenous and… Click to show full abstract

The membrane-anchored flavin mononucleotide binding domain (FBD) of CYP450 reductase was extracted in E. coli lipid-nanodiscs using charge-free pentyl-inulin polymer. FBD in nanodiscs was found to be conformationally homogenous and enabled high-resolution NMR probing. 31P NMR revealed the polymer's lack of preference for any specific E. coli lipids and identified the lipid-types in nanodiscs.

Keywords: cyp450 reductase; nanodiscs using; binding domain; coli lipid; using charge; lipid nanodiscs

Journal Title: Chemical communications
Year Published: 2022

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