Primary light harvesting system: phycobilisomes and associated membranes
Technical Report
·
OSTI ID:5775309
A comparison of the phycobilisome structure from evolutionary lower and higher red algae showed that their phycobilisome size and shape varied, but that the arrangement within the phycobilisomes was essentially the same. Allophycocyanin, the terminal phycobiliprotein in the energy transfer chain to chlorophyll, has been investigated. Two of the four allophycocyanin forms from Nostoc (cyanophyte) phycobilisomes, allophycocyanin-I and -B are the probable bridging pigments between the phycobilisomes and the photosynthetic lamellae because they have the longest absorbance and fluorescence emission forms. With procedures developed in this laboratory, vesicles with functionally attached phycobilisomes have been obtained from red and blue-green algae. These preparations have oxygen evolution rates comparable to whole cells, and show energy transfer from phycoerythrin to PS II chlorophyll with a high 695 nm (-196/sup 0/C) emission. With the availability of such preparations, and the capability of isolating phycobilisomes, probes for the phycobilisome attachment site can be undertaken. Complexes from phycobilisomes consisting of phycoerythrin and phycocyanin, which could be dissociated and recombined were further characterized. Additional polypeptide bands (with SDS-PAGE) were found only with the recombinable phycobiliprotein fractions. These polypeptides probably function in stabilizing the phycobilisome structure.
- Research Organization:
- Smithsonian Institution, Rockville, MD (USA). Radiation Biology Lab.
- DOE Contract Number:
- EY-76-S-05-4310
- OSTI ID:
- 5775309
- Report Number(s):
- ORO-4310-16
- Country of Publication:
- United States
- Language:
- English
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