The cytochrome b6f complex: structural studies and comparison with the bc1 complex
Biochimica et Biophysica Acta (BBA) - BioenergeticsPublished 1 August 2000
Cécile Breyton
Citations38
SJR quartileQ1
SJR score1.05
SNIP0.79
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TL;DR
A comparison with the structure of the bc(1) complex suggests that the transmembrane domains of the two complexes are very similar, confirming the structural homology deduced from sequence analysis.
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.
Keywords
Materials ScienceBiochemistry, Genetics and Molecular Biology
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