Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1943232 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2008 | 7 Pages |
Abstract
Heliobacteria have a Rieske/cytochrome b complex composed of a Rieske protein, a cytochrome b6, a subunit IV and a di-heme cytochrome c. The overall structure of the complex seems close to the b6f complex from cyanobacteria and chloroplasts to the exception of the di-heme cytochrome. We show here by biochemical and biophysical studies that a heme ci is covalently attached to the Rieske/cytochrome b complex from Heliobacteria. We studied the EPR signature of this heme in two different species, Heliobacterium modesticaldum and Heliobacillus mobilis. In contrast to the case of b6f complex, a strong axial ligand to the heme is present, most probably a protonatable amino acid residue.
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Authors
A.L. Ducluzeau, E. Chenu, L. Capowiez, F. Baymann,