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

Academic Article

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.
  • Published In

    Keywords

  • Animals, Cattle, Flavin Mononucleotide, Flavin-Adenine Dinucleotide, Fluorescence, Membrane Proteins, Membranes, Artificial, NADPH-Ferrihemoprotein Reductase, Nanostructures, Peptides, Phosphatidylethanolamines, Protein Conformation
  • Digital Object Identifier (doi)

    Authorlist

  • Barnaba C; Ravula T; Medina-Meza IG; Im S-C; Anantharamaiah GM; Waskell L; Ramamoorthy A
  • Start Page

  • 6336
  • End Page

  • 6339
  • Volume

  • 54
  • Issue

  • 49