Related Experiment Video
Updated: May 18, 2026

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria
Published on: November 10, 2021
Structure of a thermophilic cyanobacterial b6f-type Rieske protein
Sebastian Veit1, Kazuki Takeda, Yuichi Tsunoyama
1Plant Biochemistry, Ruhr University Bochum, 44780 Bochum, Germany.
Abstract:
The `Rieske protein' PetC is one of the key subunits of the cytochrome b(6)f complex. Its Rieske-type [2Fe-2S] cluster participates in the photosynthetic electron-transport chain. Overexpression and careful structure analysis at 2.0 Å resolution of the extrinsic soluble domain of PetC from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 enabled in-depth spectroscopic and structural characterization and suggested novel structural features. In particular, both the protein structure and the positions of the internal water molecules unexpectedly showed a higher similarity to eukaryotic PetCs than to other prokaryotic PetCs. The structure also revealed a deep pocket on the PetC surface which is oriented towards the membrane surface in the whole complex. Its surface properties suggest a binding site for a hydrophobic compound and the complete conservation of the pocket-forming residues in all known PetC sequences indicates the functional importance of this pocket in the cytochrome b(6)f complex.
Related Concept Videos
Bacterial Phylum Cyanobacteria
Electron Transport Chain: Complex III and IV
Anoxygenic Phototrophic Bacteria
Hyperthermophilic Bacteria
ATP Synthase: Structure
Diversity of Archaea III

