Studies of the orientation of the mitochondrial redox carriers. III. Orientation of the gx and gy axes of the hemes of cytochrome oxidase with respect to the plane of the membrane in oriented membrane multilayers.
The EPR absorption properties of the hemes of cytochrome oxidase and their liganded derivatives were examined in oriented multilayers from isolated oxidase, mitochondrial membranes and membrane fragments of a bacterium, Paracoccus denitrificans. The hemes of the oxidase in all the systems investigated were oriented normal to the plane of the multilayers. The directions of the g signals corresponding to the gx and gy axes of the g tensor were found to be different in low-spin ferric heme in fully oxidized oxidase and in half-reduced liganded oxidase. It is suggested that this different orientation of gx and gy in fully oxidized oxidase and half-reduced liganded oxidase arises because the respective EPR signals belong to two different hemes, those of cytochrome a and a3.
D000818:Animals; D001386:Azides; D010856:Columbidae; D003574:Cytochrome c Group; D003580:Cytochromes; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV; D006418:Heme; D007425:Intracellular Membranes / Q000201:enzymology*; D008928:Mitochondria / Q000201:enzymology*; D010084:Oxidation-Reduction; D010230:Paracoccus; D013440:Sulfides
D001386:Azides; D003574:Cytochrome c Group; D003580:Cytochromes; D013440:Sulfides; D006418:Heme; D003576:Electron Transport Complex IV