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Originally published as Biophys J. BioFAST on May 19, 2006.
doi:10.1529/biophysj.105.078501
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Biophysical Journal 91:921-926 (2006)
© 2006 The Biophysical Society

A Spatial Model of the Chromatophore Vesicles of Rhodobacter sphaeroides and the Position of the Cytochrome bc1 Complex

Tihamér Geyer and Volkhard Helms

Zentrum für Bioinformatik, Universität des Saarlandes, Saarbrücken, Germany

Correspondence: Address reprint requests to T. Geyer, Zentrum für Bioinformatik, Universität des Saarlandes, Geb. C7.1, Postfach 151150, D-66041 Saarbrücken, Germany. E-mail: tihamer.geyer{at}bioinformatik.uni-saarland.de.

The photosynthetic apparatus of purple bacteria is generally considered a well-studied and understood system. However, recent atomic force microscopy images of flattened chromatophore vesicles from Rhodobacter sphaeroides restarted a debate about the stoichiometry and positions of the membrane proteins, with the interpretations of the observed images only partly being in agreement with earlier models. The most puzzling observation from the recent images is that the Cytochrome bc1 complex, which is a central part of the photosynthetic apparatus, seems to be missing on the chromatophore vesicles, even when these were extracted from photosynthetically grown bacteria. From the available information on the geometry of the vesicle and of the proteins we reconstructed here a three-dimensional model vesicle at molecular resolution. Its central feature, also determining its diameter of ~45 nm, is an equatorial array of LH1 dimers, lined by a region of LH2 rings. This naturally puts the Cytochrome bc1 complexes and the ATPase at the vesicle's poles. This spatial model may explain why the vesicle's endcaps with the bc1 complexes are lost during the preparatory steps of the imaging process together with the ATPase and are therefore absent from the available images.




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T. Geyer
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T. Geyer and V. Helms
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