The structure of a cytochrome oxidase-lipid model membrane.
The structure of "membranous cytochrome oxidase" has been investigated by X-ray diffraction, optical polarization spectroscopy and EPR spectroscopy. These studies indicate that the cytochrome oxidase molecules are oriented symmetrically in the membrane profile with a significant portion of their mass occurring within the extravesicular surface of the membrane; the oxidase molecultes span the membrane profile; the distribution of the oxidase molecules over the plane of these membranes is non-crystalline; the oxidase molecules contain bundles of alpha-helical polypeptide chain segments where the average orientation of the helices is normal to the membrane plane; and the average heme orientation within the oxidase molecules is such that the normal to the heme plane lies in the plane of the membrane.
D000818:Animals; D010856:Columbidae; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV; D006418:Heme; D008055:Lipids; D008566:Membranes; D008928:Mitochondria / Q000201:enzymology; D011487:Protein Conformation; D013057:Spectrum Analysis; D014961:X-Ray Diffraction
D008055:Lipids; D006418:Heme; D003576:Electron Transport Complex IV