The structure of cytochrome c oxidase from Rhodobacter sphaeroides has been solved at
2.3/2.8 Å (anisotropic resolution). This high-resolution structure revealed atomic details of a …

Assembly of the core subunits of theaa 3-type cytochrome c oxidase in mitochondria and
aerobic bacteria such as Rhodobacter sphaeroides requires the association of three …

A role for conformational change in the coupling mechanism of cytochrome c oxidase is the
subject of controversy. Relatively small conformational changes have been reported in …

The catalytic core of cytochrome c oxidase is composed of three subunits: I, II, and III.
Subunit III is a highly hydrophobic membrane protein that contains no redox centers; its role …

Surf1p is a protein of the inner membrane of mitochondria that functions in the assembly of
cytochrome-c oxidase. The specifics of the role of Surf1p have remained unresolved …

To determine the interaction site for cytochromec (Cc) on cytochrome c oxidase (CcO), a
number of conserved carboxyl residues in subunit II of Rhodobacter sphaeroides CcO were …

Like many voltage-sensitive ion pumps, cytochromec oxidase is inhibited by zinc. Binding of
zinc to the outside surface of Rhodobacter sphaeroides cytochromec oxidase inhibits the …

By using the non-redox-active Mg2+/Mn2+ site of cytochrome c oxidase as a probe, water
access from the outside of the enzyme and water escape from the buried active site were …

The α proteobacter Rhodobacter sphaeroides accumulates two cytochrome c oxidases
(CcO) in its cytoplasmic membrane during aerobic growth: a mitochondrial-like aa3-type …

The identification and structural characterization of a series of ornithine lipids extracted from
the cell membranes of wild-type Rhodobacter sphaeroides, as well as from a …