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X-ray Structure of the Electron Transfer Complex between Ferredoxin and Photosystem IX-ray Structure of the Electron Transfer Complex between Ferredoxin and Photosystem I
Structural highlights
FunctionPSAF_THEVB Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI (By similarity). Publication Abstract from PubMedPhotosystem I (PSI), a large protein complex located in the thylakoid membrane, mediates the final step in light-driven electron transfer to the stromal electron carrier protein ferredoxin (Fd). Here, we report the first structural description of the PSI-Fd complex from Thermosynechococcus elongatus. The trimeric PSI complex binds three Fds in a non-equivalent manner. While each is recognized by a PSI protomer in a similar orientation, the distances between Fds and the PSI redox centres differ. Fd binding thus entails loss of the exact three-fold symmetry of the PSI's soluble subunits, inducing structural perturbations which are transferred to the lumen through PsaF. Affinity chromatography and nuclear magnetic resonance analyses of PSI-Fd complexes support the existence of two different Fd-binding states, with one Fd being more tightly bound than the others. We propose a dynamic structural basis for productive complex formation, which supports fast electron transfer between PSI and Fd. X-ray structure of an asymmetrical trimeric ferredoxin-photosystem I complex.,Kubota-Kawai H, Mutoh R, Shinmura K, Setif P, Nowaczyk MM, Rogner M, Ikegami T, Tanaka H, Kurisu G Nat Plants. 2018 Apr;4(4):218-224. doi: 10.1038/s41477-018-0130-0. Epub 2018 Apr , 2. PMID:29610537[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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