Abstract
A complex of phycobiliproteins, containing phycoerythrocyanin (PEC), C-phycovyanin (C-PC) and allo-phycocyanin (APC) as well as some linker polypeptides, was reconstructed. The absorption and fluoreacence spectra of the complex were compared with those of native phycobilisomes (PBS) and the phycobiliproteins. Based on the measured data, it can be concluded that the complex can be taken as a model of PBS and is an entirely functional group for excitation energy transfer step by step from peripheral PEC to APC. The single terminal emitter feature of the complex makes it favorable for clarifying energy transfer pathways and the kinetics in comparison with native PBS. Further research is carried on in the lab.
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