Abstract
The molecular structure-function relationship of the Fenna-Matthews-Olson light-harvesting complex of the photosynthetic green bacterium Prosthecochloris aestuarii has been investigated. It has been assumed that the electronic excited states responsible for the function (transfer of electronic excitation energy) result from the dipole-dipole interactions between the bacteriochlorophyll molecules bound to the polypeptide chain of the complex at a specific three-dimensional geometry. The molecular structure-electronic excited states relationship has been addressed on the basis of simultaneous simulations of several spectroscopic observations. Current electronic excited state models for the Fenna-Matthews-Olson complex have generally been based on obtaining an optimal match between the information contents of the optical steady-state spectra and the bacteriochlorophyll organization. Recent kinetic and spectral information gathered from ultrafast time-resolved measurements have not yet been used effectively for further refinement of the excited state models and for quantification of the relation between the excited states and the energy transfer processes. In this study, we have searched for a model that not only can explain the key features of several steady-state spectra but also the temporal and spectral evolution observed in a recent absorption difference experiment and we have discussed the implications of this model for equilibration of the electronic excitation energy in systems at low temperatures.
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Received: 12 June 1998 / Revised version: 19 October 1998 / Accepted: 30 November 1998
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Iseri, E., Gülen, D. Electronic excited states and excitation transfer kinetics in the Fenna-Matthews-Olson protein of the photosynthetic bacterium Prosthecochloris aestuarii at low temperatures. Eur Biophys J 28, 243–253 (1999). https://doi.org/10.1007/s002490050205
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DOI: https://doi.org/10.1007/s002490050205