Article
The amino-terminal portion of the Rieske iron-sulfur protein contributes to the ubihydroquinone oxidation site catalysis of the Rhodobacter capsulatus bc1 complex.
Biochemistry - 30 Sept 1997
Brasseur G, Sled V, Liebl U, Ohnishi T, Daldal F
Abstract excerpt
The Rieske iron-sulfur (Fe-S) protein subunit of bc1 complexes contains in its carboxyl-terminal part two highly conserved hexapeptide motifs (box I and box II) that include the four amino acid ligands of its [2Fe-2S] cluster. In the preceding paper [Liebl, U., Sled, V., Brasseur, G., Ohnishi, T....
Topics
- Binding Sites
- Catalysis
- Electron Spin Resonance Spectroscopy
- Electron Transport Complex III
- Escherichia coli
- Iron-Sulfur Proteins
- Models, Molecular
- Mutagenesis, Site-Directed
- Oxidation-Reduction
- Phenotype
- Rhodobacter capsulatus
- Ubiquinone