Akademik Veri Yönetim Sistemi
Turkish Journal of Physics, cilt.21, sa.11, ss.1129-1143, 1997 (Scopus)
The long-standing problem of interpretation of the spectroscopy-structure relationship of the Fenna-Matthews-Olson (FMO) protein complex from Prosthecochloris aestuarii is revisited. The main problems associated with the best current interpretations have been identified and an approach for a better-controlled solution is considered. On the conjecture that a reasonable explanation of the structure-spectroscopy relationship of the FMO should essentially result from the analysis of linear optical data that had not been employed by or available for previous studies, the low temperature (4 K) absorption and linear dichroism spectra have been simulated simultaneously using an exciton model. The model is based on the assumption that the FMO excited states that are responsible for the main function (energy transfer) are the excitonic states resulting from the dipole-dipole interactions of the individual Qy transitions among the bacteriochlorophylls of the unaggregated C3 symmetric crystalline form. On the basis of simulations, a preliminary solution to the excited state structure is provided and a strategy for further refinement is suggested. © TÜBİTAK.