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- W581483991 abstract "Photosystem 1 (PS1) is one of the two multi-subunit, pigment-protein complexes that drive the initial processes of light utilization in oxygenic photosynthesis. The PS1 complex has approximately 100 packed chlorophyll (Chl) molecules that form the antenna and functional redox cofactors comprising the reaction center (RC). The latter cofactors are arranged in two pseudo-symmetric branches, starting from P700, and then split into two branches with the ec2 and ec3 chlorophylls and phylloquinone (A1) on each branch, and then rejoin at the iron-sulfur cluster FX. All of these are bound by the heterodimer of the PsaA and PsaB subunits, while the terminal FA and FB clusters are bound by PsaC. Electron transfer (ET) along the two branches has been studied by various investigators, and it was established that both branches are active in electron transfer, but that electron transfer to FX was ~10-fold faster from PhQB than from PhQA. Recently it was suggested that the initial charge separation event can take place independently within each ec2/ec3 pair (Holzwarth et al. 2010). In order to get a clearer picture of this phenomenon, we have generated new mutations in the PsaA and PsaB subunits near the ec2 Chls. Immunoblots and optical spectroscopy were used to estimate the amount of PS1 accumulated in each mutant. We measured nanosecond optical measurements in whole cells to probe for the directionality of electron transfer in the mutants, and identified some mutations that produce an observable effect on the relative use of the two branches. We are currently investigating these by ultra-fast pump-probe spectroscopy." @default.
- W581483991 created "2016-06-24" @default.
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- W581483991 date "2012-04-01" @default.
- W581483991 modified "2023-09-25" @default.
- W581483991 title "Mutations that Affect the Directionality of Electron Transfer in Photosystem 1" @default.
- W581483991 doi "https://doi.org/10.1096/fasebj.26.1_supplement.783.1" @default.
- W581483991 hasPublicationYear "2012" @default.
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