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• W2059868052 abstract "FoF1-ATP synthase uses the electrochemical potential across membranes or ATP hydrolysis to rotate the Foc-subunit ring. To elucidate the underlying mechanism, we carried out a structural analysis focused on the active site of the thermophilic c-subunit (TFoc) ring in membranes with a solid-state NMR method developed for this purpose. We used stereo-array isotope labeling (SAIL) with a cell-free system to highlight the target. TFoc oligomers were purified using a virtual ring His tag. The membrane-reconstituted TFoc oligomer was confirmed to be a ring indistinguishable from that expressed in E. coli on the basis of the H+-translocation activity and high-speed atomic force microscopic images. For the analysis of the active site, 2D 13C-13C correlation spectra of TFoc rings labeled with SAIL-Glu and -Asn were recorded. Complete signal assignment could be performed with the aid of the Cαi+1-Cαi correlation spectrum of specifically 13C,15N-labeled TFoc rings. The Cδ chemical shift of Glu-56, which is essential for H+ translocation, and related crosspeaks revealed that its carboxyl group is protonated in the membrane, forming the H+-locked conformation with Asn-23. The chemical shift of Asp-61 Cγ of the E. coli c ring indicated an involvement of a water molecule in the H+ locking, in contrast to the involvement of Asn-23 in the TFoc ring, suggesting two different means of proton storage in the c rings." @default.
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• W2059868052 date "2014-01-01" @default.
• W2059868052 modified "2023-10-09" @default.
• W2059868052 title "Active-Site Structure of the Thermophilic Foc-Subunit Ring in Membranes Elucidated by Solid-State NMR" @default.
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• W2059868052 doi "https://doi.org/10.1016/j.bpj.2013.12.005" @default.
• W2059868052 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3907233" @default.
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