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. 1980 Apr;77(4):1961–1965. doi: 10.1073/pnas.77.4.1961

Cyanobacterial phycobilisomes: Selective dissociation monitored by fluorescence and circular dichroism

Meir Rigbi 1,*, Joanne Rosinski 1, Harold W Siegelman 1, John Clark Sutherland 1
PMCID: PMC348629  PMID: 16592802

Abstract

Phycobilisomes are supramolecular assemblies of phycobiliproteins responsible for photosynthetic light collection in red algae and cyanobacteria. They can be selectively dissociated by reduction of temperature and buffer concentration. Phycobilisomes isolated from Fremyella diplosiphon transfer energy collected by C-phycoerythrin and C-phycocyanin to allophycocyanin. The energy transfer to allophycocyanin is nearly abolished at 2°C, as indicated by a blue shift in fluorescence emission, and is accompanied by a decrease in the circular dichroism in the region of allophycocyanin absorbance. Further dissociation of the phycobilisomes can be attained by reduction of buffer concentration and holding at 2°C. Energy transfer to C-phycocyanin is nearly abolished, and decreases occur in the circular dichroism in the region of C-phycocyanin and C-phycoerythrin absorbance. Complete dissociation of the phycobilisomes at low buffer concentration and 2°C requires extended time. Energy transfer to C-phycocyanin is further reduced and the circular dichroism maximum of C-phycoerythrin at 575 nm is lost. Circular dichroism provides information on the hexamer-monomer transitions of the phycobiliproteins, whereas fluorescence is indicative of hexamer-hexamer interactions. We consider that hydrophobic interactions are fundamental to the maintenance of the structure and function of phycobilisomes.

Keywords: phycobiliproteins, energy transfer, hydrophobic interactions

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1961

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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