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| - Fluorescence Decay Kinetics of Wild Type and D2-H117N Mutant Photosystem II ReactionCenters Isolated from Chlamydomonas reinhardtii
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| - We compare the chlorophyll fluorescence decay kinetics of the wild type and the D2-H117N mutantphotosystem II reaction centers isolated from Chlamydomonas reinhardtii. The histidine residue located atsite 117 on the D2 polypeptide of photosystem II is a proposed binding site for one of two peripheral accessorychlorophylls located in the reaction center complex. The peripheral accessory chlorophylls are thought to becoupled with the primary electron donor, P680, and thus involved in energy transfer with P680. The conservativereplacement of the histidine residue with an asparagine residue allows the chlorophyll to remain bound to thereaction center. However, slight changes in the structural organization of the reaction center may exist thatcan affect the energy transfer kinetics. We show that the D2-H117N mutation causes a shift in the 20−30 pslifetime component that has been associated with energy equilibration among coupled chlorophylls in thephotosystem II reaction center.
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