Abstract
The conversion of light energy to chemical energy during photosyn-thesis involves the transfer of electrons between pigments embedded in a membrane protein. This process occurs with high quantum efficiency, the result of extremely fast electron transfer over a long distance preventing back transfer and energy loss. Recently the three-dimensional structures of the photosynthetic reaction centres of the bacteria Rhodopseudomonas viridis1 and Rhodobacter sphaeroides2 have been determined, allowing a molecular descrip-tion of the primary charge separation process. There are two symmetrically related branches of pigments in the structure (L and M), extending from the special pair of bacteriochlorophyll molecules (P) to the two bacteriopheophytins (HL and HM) via two bacteriochlorophylls (BLand BM). Many features of the electron transfer process are poorly understood, such as the nature of the excited states involved, the identity of the primary charge separation step and the roles of the protein and of B3–13. We have determined the rates of electron transfer in isolated reaction centre complexes of Rps. viridis and Rb. sphaeroides as a function of temperature. The rates increase as temperature is decreased, which may be due to either changes in electronic coupling of the pigments or changes in the population of coupled vibrational modes, or a combination of the two. We see no evidence of a B−L intermediate, which sets a lower limit on the rate of electron transfer from BL to HL. This is so high as to rule out transfer by two non-adiabatic steps.
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Fleming, G., Martin, J. & Breton, J. Rates of primary electron transfer in photosynthetic reaction centres and their mechanistic implications. Nature 333, 190–192 (1988). https://doi.org/10.1038/333190a0
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DOI: https://doi.org/10.1038/333190a0
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