Premium
THE DEVELOPMENT OF EXCITON MIGRATION ROUTES FOR PHYCOCYANIN 645 AND ALLOPHYCOCYANIN
Author(s) -
Csatorday Karoly,
GuardFriar Deborah,
MacColl Robert,
Berns Donald S.
Publication year - 1988
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1988.tb02728.x
Subject(s) - allophycocyanin , exciton , phycocyanin , absorption spectroscopy , spectral line , molecular physics , dipole , fluorescence , chemistry , absorption (acoustics) , absorption band , chemical physics , photochemistry , physics , optics , biology , condensed matter physics , quantum mechanics , genetics , cyanobacteria , organic chemistry , bacteria
— The origin of the comparatively complex absorption spectrum of the cryptomonad biliprotein, phycocyanin 645 from Chroomonas species, has been investigated by deconvolution of its absorption and CD spectra together with fluorescence polarization studies. The visible absorption and CD spectra were each deconvoluted into four components, three pure Gaussian and one Gaussian‐Lorentzian chimera. The difference spectrum between the visible absorption spectra of partially renatured and partially dissociated protein and the fluorescence polarization spectrum are compared to these deconvolutions. All results are consistent with a previous proposal that band splitting from a pair of strongly‐coupled dipoles contributes to the absorption and CD spectra of this biliprotein. A model for the flow of exciton migration through this protein is presented that incorporates these data [together with appropriate literature reports]. This exciton migration model together with one for the biliprotein, allophycocyanin, includes both strong and very weak coupling of dipoles. This combination of mechanisms has salient influence on the visible absorption spectra and the routes of exciton migration characteristic of these two proteins.