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- W1970285247 abstract "FoF1-ATP synthase catalyzes ATP synthesis coupled with proton-translocation across the membrane. The membrane-embedded Fo portion is responsible for the H+ translocation coupled with rotation of the oligomeric c-subunit ring, which induces rotation of the γ subunit of F1. For solid-state NMR measurements, FoF1 of thermophilic Bacillus PS3 (TFoF1) was overexpressed in Escherichia coli and the intact c-subunit ring (TFoc-ring) was isolated by new procedures. One of the key improvement in this purification was the introduction of a His residue to each c-subunit that acts as a virtual His10-tag of the c-ring. After solubilization from membranes by sodium deoxycholate, the c-ring was purified by Ni–NTA affinity chromatography, followed by anion-exchange chromatography. The intactness of the isolated c-ring was confirmed by high-resolution clear native PAGE, sedimentation analysis, and H+-translocation activity. The isotope-labeled intact TFoc-ring was successfully purified in such an amount as enough for solid-state NMR measurements. The isolated TFoc-rings were reconstituted into lipid membranes. A solid-state NMR spectrum at a high quality was obtained with this membrane sample, revealing that this purification procedure was suitable for the investigation by solid-state NMR. The purification method developed here can also be used for other physicochemical investigations." @default.
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- W1970285247 date "2012-04-01" @default.
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- W1970285247 title "Purification, characterization and reconstitution into membranes of the oligomeric c-subunit ring of thermophilic FoF1-ATP synthase expressed in Escherichia coli" @default.
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- W1970285247 doi "https://doi.org/10.1016/j.pep.2012.02.005" @default.
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