In the first part,the energy transfer pathways in trimeric and hexameric aggregation state of cyanobacteria C-phycocyanin(C-PC)were investigated in the framework of F rster model.Only when the protonation of phycocyanobilins and their long-and short-rang interactions were properly taken into account,the calculated energy transfer rates were in good agreement with the experimental results of C-PC monomer and trimer.In C-PC hexamer,an additional energy flow were predicted to be from β-155 in top trimer to adjacent β-155 in bottom trimer(Figure1).Fructose-1,6-/sedoheptulose-1,7-bisphosphatase(C-FBP/SBPase)is a unique enzyme for cyanobacteria with essential roles in Calvin Cycle.Structural and biochemical characterization of C-FBP/SBPase from the Synechocystis strain 6803 have been reported in the second part.With a systematically structure-centric approach,we identified the first set of novel dual-target inhibitors against cyanobacterial fructose-1,6-bisphosphate aldolase(FBA)and C-FBP/SBPase.The obtained inhibitors show micromolar-range activities in vitro and in vivo,and may open a promising route towards developing environmentally acceptable chemical control for cyanobacteria blooms treatment.