Abstract
The transfer and trapping of excitation energy in a variety of photosynthetic bacteria was investigated using steady-state and time-resolved polarized light spectroscopy. The experiments at room temperature show that equilibration of the excitation density among different antenna pools is the dominant process before trapping or losses occur. Only at extremely high light-intensities effects due to multiphoton processes are observed, which indicate that in many of these bacterial systems the excitons can diffuse over a 1000 pigments or more before their disappearance.
The main antenna pigment-protein complex, B875, is not homogeneous, but contains a minor spectral form, B896, absorbing between 890 and 900 nm dependent on the temperature. B896 is the terminal excitation acceptor, before transfer to the reaction center occurs. At 77 K transfer from B875 to B896 and from B896 to the reaction center was studied. The former takes 20 ps, while the latter transfer step occurs within about 40 ps. This implies that B896 is situated at a distance of 2.5—3.0 nm from the special pair.
The function of B896 is probably to act as a focus for the excitations and to provide a specific entry into the reaction center. This may be a general feature in photosythetic systems.
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Van Grondelle, R., Bergström, H., Sundström, V. (1991). Trapping of Excitation Energy in Photosynthetic Purple Bacteria. In: Riklis, E. (eds) Photobiology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3732-8_39
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DOI: https://doi.org/10.1007/978-1-4615-3732-8_39
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