title: Membrane topology of microsomal cytochrome P-450: saturation transfer EPR and freeze-fracture electron microscopy studies.
abstract: The rotation of cytochrome P-450 LM2 (CYPIIB4) incorporated into large microsomal-like lipid vesicles was investigated by saturation transfer EPR using 15N- and 2H-substituted spin labels. In combination with rotational diffusion, the distribution and size of protein particles in the bilayer were studied by freeze-fracture electron microscopy. The data from both methods suggest an oligomeric and membrane-spanning aggregate for the topology of microsomal cytochrome P-450.
authors.affiliation: Central Institute for Molecular Biology, Academy of Sciences of GDR, Berlin-Buch.
authors.forename: D
authors.initials: D
authors.lastname: Schwarz
authors.forename: J
authors.initials: J
authors.lastname: Pirrwitz
authors.forename: H W
authors.initials: HW
authors.lastname: Meyer
authors.forename: M J
authors.initials: MJ
authors.lastname: Coon
authors.forename: K
authors.initials: K
authors.lastname: Ruckpaul
mesh_terms: D003577:Cytochrome P-450 Enzyme System; D004058:Diffusion; D004578:Electron Spin Resonance Spectroscopy; D005614:Freeze Fracturing; D066298:In Vitro Techniques; D008854:Microscopy, Electron; D008861:Microsomes / Q000201:enzymology* / Q000648:ultrastructure; D009038:Motion
chemical_list: D003577:Cytochrome P-450 Enzyme System