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Peer-reviewedCC BY 4.0Biochimica biophysica acta (BBA) - Bioenergetics

The Rieske/cytochrome b complex of Heliobacteria

  • A.L. Ducluzeau
  • E. Chenu
  • L. Capowiez
  • Frauke Baymann
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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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Cite

BibTeXRIS
BibTeX
@article{ducluzeau2026rieskecytochrome,
  title = {{The Rieske/cytochrome b complex of Heliobacteria}},
  author = {A.L. Ducluzeau and E. Chenu and L. Capowiez and Frauke Baymann},
  journal = {Biochimica biophysica acta (BBA) - Bioenergetics},
  year = {2026},
  month = sep,
  doi = {10.1016/j.bbabio.2008.04.026},
  url = {https://hal.science/hal-05741387v1},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - The Rieske/cytochrome b complex of Heliobacteria
AU  - A.L. Ducluzeau
AU  - E. Chenu
AU  - L. Capowiez
AU  - Frauke Baymann
PY  - 2026
DA  - 2026/09/07
JO  - Biochimica biophysica acta (BBA) - Bioenergetics
DO  - 10.1016/j.bbabio.2008.04.026
UR  - https://hal.science/hal-05741387v1
AB  - 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.
SN  - 0005-2728
SN  - 1879-2650
ER  -