Abstract
C-phycocyanin and allophycocyanin are light-harvesting proteins that occur in the phycobilisome in cyanobacteria.1 They represent relatively simple systems in which the structural factors that govern the direction and rate of excitation transfer can be addressed through the methods of picosec-ond spectroscopy. Several aspects of the structure of C-phycocyanin, as recently determined by X-ray crystallographic methods,2 present challenges to current theories for excitation transfer in light-harvesting proteins. We have begun a detailed characterization of the picosecond transient absorption and dichroism kinetics of C-phycocyanin in order to compare measured patterns of excitation transfer in C-phycocyanin with those indicated by direct calculation, using the known coordinates and orientations of the pigment molecules bound by the protein. We are also examining excitation transfer processes in allophycocyanin, a similar phycobiliprotein that directs excitation energy received from C-phycocyanin towards the photosystem II reaction center.
© 1990 Optical Society of America
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