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Lipid-exchange in nanodiscs discloses membrane boundaries of cytochrome-P450 reductase
- Source :
- Chemical Communications. 54:6336-6339
- Publication Year :
- 2018
- Publisher :
- Royal Society of Chemistry (RSC), 2018.
-
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.
- Subjects :
- 0301 basic medicine
Oxygenase
Flavin Mononucleotide
Protein Conformation
Article
Fluorescence
Catalysis
03 medical and health sciences
chemistry.chemical_compound
Ethanolamine
Protein structure
Materials Chemistry
Animals
Transferase
NADPH-Ferrihemoprotein Reductase
Phosphatidylethanolamines
Metals and Alloys
Membrane Proteins
Cytochrome P450 reductase
Membranes, Artificial
General Chemistry
Nanostructures
Surfaces, Coatings and Films
Electronic, Optical and Magnetic Materials
030104 developmental biology
Membrane
chemistry
Membrane protein
Flavin-Adenine Dinucleotide
Ceramics and Composites
Microsome
Biophysics
Cattle
Peptides
Subjects
Details
- ISSN :
- 1364548X and 13597345
- Volume :
- 54
- Database :
- OpenAIRE
- Journal :
- Chemical Communications
- Accession number :
- edsair.doi.dedup.....4158b1e87c41084a77cddbdea82d4f55