Photosynthesis Research

, Volume 104, Issue 2, pp 233–243

A model of the protein–pigment baseplate complex in chlorosomes of photosynthetic green bacteria

  • Marie Ø. Pedersen
  • Juha Linnanto
  • Niels-Ulrik Frigaard
  • Niels Chr. Nielsen
  • Mette Miller
Review

DOI: 10.1007/s11120-009-9519-y

Cite this article as:
Pedersen, M.Ø., Linnanto, J., Frigaard, NU. et al. Photosynth Res (2010) 104: 233. doi:10.1007/s11120-009-9519-y

Abstract

In contrast to photosynthetic reaction centers, which share the same structural architecture, more variety is found in the light-harvesting antenna systems of phototrophic organisms. The largest antenna system described, so far, is the chlorosome found in anoxygenic green bacteria, as well as in a recently discovered aerobic phototroph. Chlorosomes are the only antenna system, in which the major light-harvesting pigments are organized in self-assembled supramolecular aggregates rather than on protein scaffolds. This unique feature is believed to explain why some green bacteria are able to carry out photosynthesis at very low light intensities. Encasing the chlorosome pigments is a protein-lipid monolayer including an additional antenna complex: the baseplate, a two-dimensional paracrystalline structure containing the chlorosome protein CsmA and bacteriochlorophyll a (BChl a). In this article, we review current knowledge of the baseplate antenna complex, which physically and functionally connects the chlorosome pigments to the reaction centers via the Fenna–Matthews–Olson protein, with special emphasis on the well-studied green sulfur bacterium Chlorobaculum tepidum (previously Chlorobium tepidum). A possible role for the baseplate in the biogenesis of chlorosomes is discussed. In the final part, we present a structural model of the baseplate through combination of a recent NMR structure of CsmA and simulation of circular dichroism and optical spectra for the CsmA–BChl a complex.

Keywords

ChlorosomeBaseplateCsmAMolecular modelingPhotosynthetic antenna

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Marie Ø. Pedersen
    • 1
    • 2
  • Juha Linnanto
    • 3
  • Niels-Ulrik Frigaard
    • 4
  • Niels Chr. Nielsen
    • 1
    • 2
  • Mette Miller
    • 5
  1. 1.Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO)Aarhus UniversityArhus C, AarhusDenmark
  2. 2.Department of ChemistryAarhus UniversityArhus C, AarhusDenmark
  3. 3.Department of ChemistryUniversity of JyväskyläJyvaskylaFinland
  4. 4.Department of BiologyUniversity of CopenhagenCopenhagen NDenmark
  5. 5.Department of Biochemistry and Molecular BiologyUniversity of Southern DenmarkOdense MDenmark