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Biochim Biophys Acta. 2000 Aug 15;1459(2-3):467-74.

The cytochrome b(6)f complex: structural studies and comparison with the bc(1) complex.

Author information

1
Max-Planck Institute of Biophysics, Department of Structural Biology, Heinrich-Hoffmann-Strasse 7, D-60528, Frankfurt am Main, Germany. breyton@mpibp-frankfurt.mpg.de

Abstract

Electron crystallography of the chloroplastic b(6)f 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 bc(1) complex, the mitochondrial homologue of the b(6)f 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 b(6)f as in the bc(1) complex upon the binding of the quinol analogue stigmatellin. Crystallographic data also suggest movements in the transmembrane domains of the b(6)f complex, which would be specific of the b(6)f complex.

PMID:
11004464
DOI:
10.1016/s0005-2728(00)00185-7
[Indexed for MEDLINE]
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