Studies on the orientations of the mitochondrial redox carriers. I. Orientation of the hemes of cytochrome c oxidase with respect to the plane of a cytochrome oxidase-lipid model membrane.
The liganded derivatives of mitochondrial cytochrome c oxidase have been prepared in hydrated oriented multilayers of membranous cytochrome c oxidase. The optical spectra of the liganded derivatives recorded at an angle of 45 degrees between the incident light beam and the normal to the planes of the membranes in the multilayers show dichroic ratios of almost 2 in the visible region and 1.2-1.4 in the Soret region. The dichroic ratios were found to be similar for both cytochromes a and a3. Electron paramagnetic resonance spectra of the azide, sulfide, and formate complexes of cytochrome c oxidase obtained as a function of the orientation of the applied magnetic field relative to the planes of the membranes in the multilayer confirm the optical data and demonstrate that both hemes of cytochrome c oxidase are oriented such that the angle between the heme normal and the membrane normal is approximately 90 degrees.
D000818:Animals; D001386:Azides; D002248:Carbon Monoxide; D010856:Columbidae; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV; D005561:Formates; D005615:Freezing; D006418:Heme; D008055:Lipids; D008567:Membranes, Artificial; D008928:Mitochondria / Q000201:enzymology*; D013053:Spectrophotometry; D013440:Sulfides
D001386:Azides; D005561:Formates; D008055:Lipids; D008567:Membranes, Artificial; D013440:Sulfides; D006418:Heme; D002248:Carbon Monoxide; D003576:Electron Transport Complex IV