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Biochim Biophys Acta. 2009 Apr;1787(4):272-9. doi: 10.1016/j.bbabio.2009.01.009. Epub 2009 Jan 22.

Structural organisation of phycobilisomes from Synechocystis sp. strain PCC6803 and their interaction with the membrane.

Author information

1
Department of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.

Abstract

In cyanobacteria, the harvesting of light energy for photosynthesis is mainly carried out by the phycobilisome - a giant, multi-subunit pigment-protein complex. This complex is composed of heterodimeric phycobiliproteins that are assembled with the aid of linker polypeptides such that light absorption and energy transfer to photosystem II are optimised. In this work we have studied, using single particle electron microscopy, the phycobilisome structure in mutants lacking either two or all three of the phycocyanin hexamers. The images presented give much greater detail than those previously published, and in the best two-dimensional projection maps a resolution of 13 A was achieved. As well as giving a better overall picture of the assembly of phycobilisomes, these results reveal new details of the association of allophycocyanin trimers within the core. Insights are gained into the attachment of this core to the membrane surface, essential for efficient energy transfer to photosystem II. Comparison of projection maps of phycobilisomes with and without reconstituted ferredoxin:NADP oxidoreductase suggests a location for this enzyme within the complex at the rod-core interface.

PMID:
19344661
DOI:
10.1016/j.bbabio.2009.01.009
[Indexed for MEDLINE]
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