Evidence for various degrees of motional freedom of the "boundary" lipid in cytochrome oxidase.
The cytochrome oxidase-lipid complex from beef heart mitochondria after various degrees of lipid extraction has been studied by electron spin resonance spectroscopy using spin labelled fatty acids and phospholipids. With cytochrome oxidase at the lowest lipid content (below 0.2 mg/mg of protein) i.e. at the level sometimes referred to as the "boundary" lipid, with spin labelled fatty acids an immobilized spectrum is observed. However, when spin labelled phospholipids are used under the same conditions, a mobile component is also observed. A quantitative estimation of the spectral components by computer analysis has been performed. The difference in behaviour of the spin labelled fatty acids and phospholipids suggest that the part of the residual lipid of the complex, which in some conditions is apparently immobilised, may exhibit in other conditons a considerably high degree of mobility.
D000818:Animals; D002417:Cattle; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV; D007425:Intracellular Membranes / Q000201:enzymology; D008563:Membrane Lipids; D008565:Membrane Proteins; D008929:Mitochondria, Heart / Q000201:enzymology*; D010743:Phospholipids; D013499:Surface Properties
D008563:Membrane Lipids; D008565:Membrane Proteins; D010743:Phospholipids; D003576:Electron Transport Complex IV