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 fluorescence spect
ra of the complex were compared with those of native phycobilisomes (P
BS) and the phycobiliproteins. Based on the measured data, it can be c
oncluded that the complex can he taken as a model of PBS and is an ent
irely functional group for excitation energy transfer step by step fro
m peripheral PEC to APC. The single terminal emitter feature of the co
mplex makes it favorable for clarifying energy transfer pathways and t
he kinetics in comparison with native PBS. Further research is carried
on in the lab.