Abstract
Heliobacteria have a Rieske/cytochrome b complex composed of a Rieske protein, a cytochrome b 6, a subunit IV and a di-heme cytochrome c. The overall structure of the complex seems close to the b 6 f complex from cyanobacteria and chloroplasts to the exception of the di-heme cytochrome. We show here by biochemical and biophysical studies that a heme c i 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 b 6 f complex, a strong axial ligand to the heme is present, most probably a protonatable amino acid residue.
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