Pump-probe anisotropies of Fenna-Matthews-Olson protein trimers from Chlorobium tepidum: a diagnostic for exciton localization?
Exciton calculations on symmetric and asymmetric Fenna-Matthews-Olson (FMO) trimers, combined with absorption difference anisotropy measurements on FMO trimers from the green bacterium Chlorobium tepidum, suggest that real samples exhibit sufficient diagonal energy disorder so that their laser-excited exciton states are noticeably localized. Our observed anisotropies are clearly inconsistent with 21-pigment exciton simulations based on a threefold-symmetric FMO protein. They are more consistent with a 7-pigment model that assumes that the laser-prepared states are localized within a subunit of the trimer. Differential diagonal energy shifts of 50 cm(-1) between symmetry-related pigments in different subunits are large enough to cause sharp localization in the stationary states; these shifts are commensurate with the approximately 95 cm(-1) inhomogeneous linewidth of the lowest exciton levels. Experimental anisotropies (and by implication steady-state linear and circular dichroism) likely arise from statistical averaging over states with widely contrasting values of these observables, in consequence of their sensitivity to diagonal energy disorder.
Savikhin
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U.S. Department of Energy, and Department of Chemistry, Iowa State University, Ames 50011, USA.
Buck
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Struve
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D016880:Anisotropy; D001426:Bacterial Proteins; D055592:Biophysical Phenomena; D001703:Biophysics; D019414:Chlorobi / Q000737:chemistry; D004735:Energy Transfer; D045342:Light-Harvesting Protein Complexes; D008956:Models, Chemical; D010777:Photochemistry; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000528:radiation effects*; D011487:Protein Conformation
D001426:Bacterial Proteins; C086320:FMO bacteriochlorophyll protein, Bacteria; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins