English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

The cytochrome b6 f complex: structural studies and comparison with the bc1 complex

MPS-Authors
/persons/resource/persons251710

Breyton,  Cécile
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Breyton, C. (2000). The cytochrome b6 f complex: structural studies and comparison with the bc1 complex. Biochimica et Biophysica Acta, Bioenergetics, 1549(2-3), 467-474. doi:10.1016/S0005-2728(00)00185-7.


Cite as: http://hdl.handle.net/21.11116/0000-0007-CD7D-7
Abstract
Electron crystallography of the chloroplastic b6f complex allowed the calculation of projection maps of crystals negatively stained or embedded in glucose. This gives insights into the overall structure of the extra- and transmembrane domains of the complex. A comparison with the structure of the bc1 complex, the mitochondrial homologue of the b6f complex, suggests that the transmembrane domains of the two complexes are very similar, confirming the structural homology deduced from sequence analysis. On the other hand, the extramembrane organisation of the c-type cytochrome and of the Rieske protein seems quite different. Nevertheless, the same type of movement of the Rieske protein is observed in the b6f as in the bc1 complex upon the binding of the quinol analogue stigmatellin. Crystallographic data also suggest movements in the transmembrane domains of the b6f complex, which would be specific of the b6f complex.