Quarternary Structure of the B875 Light-Harvesting Complex from Rhodospirillum Rubrum G9+

  • R. Ghosh
  • J. Kessi
  • H. Hauser
  • E. Wehrli
  • R. Bachofen
Part of the FEMS Symposium book series (FEMSS)

Abstract

The structure of the light-harvesting complexes in purple non-sulphur bacteria is a subject of intense research at present (see Zuber, 1985). A particularly well-characterized example is the B875 complex from Rhodospirillum rubrum. The single type of light-harvesting complex (B875) in this organism is formed from two non-identical polypeptides, α and β, respectively, and possess 2 mol bacteriochlorophyll (BCh1) and 1 mol spirilloxanthin/mol αβ dimer, respectively (Picorel et al. 1983). The sequences and topology of the complex have been determined (Brunishoiz et al. 1984, Meister et al. 1985, Brunisholz et al. 1986, Bachofen and Wiemken, 1986). However, the quarternary structure of the complex is a subject of some controversy (Miller et al. 1987, Ghosh et al. 1988, Hunter et al. 1988). Recently Loach and coworkers isolated a complex absorbing at 820nm (B820) which was suggested to be a subunit form of the B875 complex. However, the precise molecular weight of the complex and its in vivo significance remained unclear. In this paper we examine the molecular properties of the B820 complex in more detail and suggest a possible model for the role of the B820 complex in vivo.

Keywords

B875 Complex Analytical Ultracentrifugation Rhodospirillum Rubrum B868 Unit Reconstituted Membrane 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bachofen, R. and Wiemken, V. (1986) Encycl. Plant Physiol. 19, 620–631.Google Scholar
  2. Brunisholz, R. A., Suter, F. and Zuber, H. (1984) Hoppe-Seyler’s Z. Physiol. Chemie 365, 675–688.CrossRefGoogle Scholar
  3. Brunisholz, R. A., Zuber, H., Valentine, J., Lindsay, J. G., Woolley, K. J. and Cogdell, R. J. (1986) Biochim. Biophys. Acta 849, 295–303.CrossRefGoogle Scholar
  4. Ghosh, R., Hauser, H. and Bachofen, R. (1988) Biochemistry 27, 1004–1014.CrossRefGoogle Scholar
  5. Hunter, C. N., Pennoyer, J. D., Sturgis, J. N., Farrelly, D. and Niederman, R. A. (1988) Biochemistry 27, 3459–3467.CrossRefGoogle Scholar
  6. McPherson, A. (1982) Preparation and Analysis of Protein Crystals, Wiley-Interscience.Google Scholar
  7. Meister, H.-P., Bachofen, R., Semenza, G. and Brunner, J. (1985) J. Biol. Chem. 260, 16326–16331.PubMedGoogle Scholar
  8. Miller, J. F., Hinchigeri, S. B., Parkes-Loach, P. S., Callaghan, P. M., Sprinkle, J. R., Riccobono, J. R. and Loach, P. A. (1987) Biochemistry 26, 5055–5062.PubMedCrossRefGoogle Scholar
  9. Parkes-Loach, P. S., Sprinkle, J. R. and Loach, P. A. (1988) Biochemistry 27, 2718–2727.PubMedCrossRefGoogle Scholar
  10. Peterson, G.L. (1977) Analyt. Biochem. 83, 346–356.PubMedCrossRefGoogle Scholar
  11. Picorel, R., Belanger, G. and Gingras, G. (1983) Biochemistry 22, 2491–2497.CrossRefGoogle Scholar
  12. Rosenbach-Belkin, V., Braun, P. and Scherz, A. (1988) in: Photosynthetic Light-Harvesting Systems (Scheer H. and Schneider S., eds), Walter de Gruyter, Berlin, p. 323–325.Google Scholar
  13. Zuber, H. (1985) Photochem. Photobiol. 42, 821–844.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • R. Ghosh
    • 1
  • J. Kessi
    • 2
  • H. Hauser
    • 2
  • E. Wehrli
    • 3
  • R. Bachofen
    • 1
  1. 1.Institute for Plant BiologyUniversity of ZürichZürichSwitzerland
  2. 2.Laboratory for BiochemistryETH-ZürichZürichSwitzerland
  3. 3.Department for Electron MicroscopyETH-ZürichZürichSwitzerland

Personalised recommendations