PHYCOERYTHROCYANIN: ITS SPECTROSCOPIC BEHAVIOR AND PROPERTIES

Abstract

Abstract— Phycoerythrocyanin is a biliprotein found in very few blue‐green algae. Its properties have been examined under three conditions: in whole cells, in light‐harvesting organelles (the phycobilisomes). and as an isolated protein. Absorption and fluorescence bands characteristic of the isolated protein are essentially the same as those in intact cells of the blue‐green alga Anabaena variabilis. The same spectroscopic hallmarks are observed in purified phycobilisomes. Dissociation of these physobilisomes at low‐phosphate concentrations resulted in increased phycoerythrocyanin fluorescence. This time‐dependent increase in fluorescence demonstrates the function of this biliprotein in excitation‐energy transfer to the other biliproteins when the organelles are intact. The relative stabilities of the various heteroprotein bonds within the phycobilisomes are shown to possess differing phosphate ion dependencies. Studies on the isolated protein from Mastigocladus laminosus include fluorescence measurements at both 23 and‐196°C, as is generally observed with biliproteins, although phycoerythrocyanin has complex visible absorption and excitation spectra, only a single emission band is observed.