We have used various techniques for preparation of specimens for electron microscopy in order to selectively contrast different regions of vesicle crystals of cytochrome c oxidase dimers. The results are consistent with a dimer composed of two y-shaped monomers [Fuller et al., J. Mol. Biol. 134 (1979) 305] aligned along one pair of arms with the other pair of arms approximately 70 Å apart. The four arms of the monomers lie within and perpendicular to the lipid bilayer in which the dimer is embedded, and the arms protrude approximately 25 Å from the lipid bilayer on the matrix side of the membrane. The cytoplasmic side domains of the two monomers split away from one another forming a large cleft in the dimer. Monovalent antibodies (Fab fragments) to subunit IV appear to bind to the two monomer arms which are closely apposed across the two-fold axis of the dimer.
|Original language||English (US)|
|Number of pages||7|
|State||Published - 1984|
ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- Atomic and Molecular Physics, and Optics