Bacterial photosynthesis begins with quantum-mechanical coherence.
In the antenna system of photosynthetic bacteria, pigments form circular aggregates whose excitations are excitons with quantum-mechanical coherence extending over many pigments. These excitons play crucial roles in light harvesting, storage, and excitation-energy transfer (EET). EET takes place rapidly to and/or from optically forbidden exciton states, without total transition dipole, within the antenna system and to the reaction center. Such EETs cannot be rationalized by Förster's formula, the traditional theory on EET, because it allows EET only between optically allowed states. The coherence in the excitons seems to prohibit rapid EET on this formula. The bacteria overcome this difficulty by circumventing the coherence, using the effects of the physical size of an aggregate that is larger than the shortest distance between pigments in the donor and pigments in the acceptor. The shortest-distance pair therein cannot detect whether the aggregate has a nonvanishing total transition dipole or not, since the pair see effectively only the transition dipole on the other pigment in themselves. The transition dipole facilitates rapid EET even to and/or from optically forbidden exciton states. Such EETs have enabled us to develop a general formula for the rate constant of EET. This is a formula in the weak-interaction limit, and so is Förster's formula, but it correctly takes into account the above size effect.
Sumi
H
H
Institute of Materials Science, University of Tsukuba, Japan. sumi@ims.tsukuba.ac.jp
D001429:Bacteriochlorophylls / Q000737:chemistry* / Q000378:metabolism; D045342:Light-Harvesting Protein Complexes; D008954:Models, Biological; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry / Q000378:metabolism; D011789:Quantum Theory; D012247:Rhodospirillum rubrum / Q000378:metabolism*
D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins