Electron microscopic characterization of helical filaments formed by subunits I and II (core proteins) of ubiquinol: cytochrome c reductase from Neurospora mitochondria.

The isolated and water-soluble complex of subunits I and II (core proteins) of ubiquinone:cytochrome c reductase from Neurospora mitochondria forms filaments below pH 6.0. Three independent helical reconstructions of single filaments were compared with the 3-D reconstruction of the native enzyme. A model for the helix is proposed in which the core complex dimers are arranged radially with the face which is proximal to the membrane in the native enzyme on the outside of the helix. The dimension of the core complex dimer perpendicular to the helix axis (70 A) provides an independent estimate of the height of the core complex to that obtained previously from cytochrome reductase crystals. The results of STEM mass measurement and the helical model give a mass per repeating unit of 90 kDa, which would indicate that the monomeric core complex consists of one 45-kDa and one 50-kDa subunit.