Labelling of the subunits of the mitochondrial adenosine triphosphatase complex in contact with the lipid bilayer [proceedings].
Explore the source record for details and available documents.
Biomedical subjects
Publications and source records attributed to R Bisson.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Cytochrome c derivatives labeled with a 3-nitrophenylazido group at lysine 13, at lysine 22, or at both residues have been prepared. The interaction of the cytochrome c derivatives with beef heart cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) in the presence of ultrviolet light results in formation of a covalent complex between cytochrome c and the oxidase. Using the lysine 22 derivative, the polypeptide composition of the oxidase is not modified, nor is its catalytic activity, whereas with the lysine 13 derivative, the gel electrophoretic pattern is altered and the catalytic activity of the complex diminished. The data are consisten with a specfic covalent interaction of the lysine 13 derivative of cytochrome c with the polypeptide of molecular weight 23,700 (Subunit II) of cytochrome c oxidase.
Explore the source record for details and available documents.
An arrangement for the membrane-spanning segments of the three larger subunits of cytochrome c oxidase is proposed on the basis of sequence comparison and polarity distribution estimated from the data available for 11 different organisms.