Membrane topology of microsomal cytochrome P-450: saturation transfer EPR and freeze-fracture electron microscopy studies.
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.
Schwarz
D
D
Central Institute for Molecular Biology, Academy of Sciences of GDR, Berlin-Buch.
Pirrwitz
J
J
Meyer
H W
HW
Coon
M J
MJ
Ruckpaul
K
K
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
D003577:Cytochrome P-450 Enzyme System