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Organization and Assembly of Light-Harvesting Complexes in the Purple Bacterial Membrane

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The Purple Phototrophic Bacteria

Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 28))

Summary

Recent in situ surface images of the intracytoplasmic membrane (ICM) of purple photosynthetic bacteria obtained at submolecular resolution by atomic force microscopy (AFM), have revealed multiple, species-dependent patterns of supramolecular organizations for their light-harvesting (LH) antennas, suggested earlier from spectroscopic studies. These have varied from highly ordered linear arrays of dimeric reaction center-light-harvesting 1-PufX (RC-LH1-PufX) core complexes in Rhodobacter (Rba.) sphaeroides, with the peripheral LH2 antenna either interspersed between them or arranged in larger clusters, to a less orderly arrangement found in several other purple bacteria, in which randomly organized, monomeric RC-LH1-enriched domains co-exist with large, paracrystalline hexagonally packed LH2 domains. In addition, regions with apparently crystalline core complexes were observed in Rhodopseudomonas (Rps.) palustris, along with a protein-free lipid bilayer. Likely bases for the absence of the ATP synthase and cytochrome bc 1 complex from the AFM topographs are discussed, including the possibility that they localize at the poles of ICM vesicles either out of view of flat regions imaged by AFM, or are removed during membrane preparation. We also discuss how the observed arrangements of LH2 and core complexes may specifically control quinol escape from the RC, emphasizing the importance of short-range diffusion within the disordered regions of the membrane in promoting the passage of quinone, and how this process may be augmented by quinone exclusion from large, ordered fields of the LH2 antenna. Possible forces that drive in vitro autoassembly of LH complexes are assessed along with the roles that complex-specific and general membrane assembly factors may play in driving the assembly and organization of photosynthetic units within the cell. Finally, we address likely perspectives for further studies on the organization and assembly of bacterial antenna complexes over the next decade.

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Abbreviations

2-D:

2-dimensional

AFM:

atomic force microscopy

bc1 complex:

ubiquinol-cytochrome c 2oxidoreductase

BChl:

bacteriochlorophyll a

Blc. :

Blastochloris

BP:

bacteriophytochrome

CM:

cytoplasmic membrane

E. :

Eschericha

ICM:

intracytoplasmic membrane

LD:

linear dichroism

LH:

light-harvesting

LH1:

core light-harvesting complex

LH2:

peripheral light-harvesting complex

Phs. :

Phaeospirillum

PS II:

Photosystem II

PSU:

photosynthetic unit consisting of LH1-reaction center core structures with LH2 arranged at their peripheries

Rba. :

Rhodobacter

RC:

reaction center

Rps. :

Rhodopseudomonas

Rsp. :

Rhodospirillum

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Authors and Affiliations

  1. Laboratoire d’Ingénierie des Systèmes Macromoléculaires, UPR 9027, Institute de Biologie Structurale et Microbiologie, CNRS, 31 Chemin Joseph Aiguier, 13402, Marseille, France

    James N. Sturgis

  2. Department of Molecular Biology and Biochemistry, Nelson Biological Laboratories, Rutgers University, 604 Allison Road, Piscataway, NJ, 08854-8082, USA

    Robert A. Niederman

Authors
  1. James N. Sturgis
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  2. Robert A. Niederman
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Correspondence to Robert A. Niederman .

Editor information

Editors and Affiliations

  1. University of Sheffield, UK

    C. Neil Hunter

  2. University of Pennsylvania, USA

    Fevzi Daldal

  3. Argonne National Laboratory, USA

    Marion C. Thurnauer

  4. University of British Columbia, Canada

    J. Thomas Beatty

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© 2009 Springer Science + Business Media B.V

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Sturgis, J.N., Niederman, R.A. (2009). Organization and Assembly of Light-Harvesting Complexes in the Purple Bacterial Membrane. In: Hunter, C.N., Daldal, F., Thurnauer, M.C., Beatty, J.T. (eds) The Purple Phototrophic Bacteria. Advances in Photosynthesis and Respiration, vol 28. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-8815-5_14

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