Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 278, Issue 8, Pages 6066-6074Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M210199200
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- NIGMS NIH HHS [GM23105, 5T32 GM08349] Funding Source: Medline
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The role of subunit a in proton translocation by the Escherichia coli F1F0. ATP synthase is poorly understood. In the membrane-bound F-o sector of the enzyme, H+ binding and release occurs at Asp(61) in the middle of the second transmembrane helix (TMH) of subunit c. Protons are thought to reach Asp(61) via an aqueous access pathway formed at least in part by one or more of the five TMHs of subunit a. In this report, we have substituted Cys into a 19-residue span of the fourth TMH of subunit a and used chemical modification to obtain information about the aqueous accessibility of residues along this helix. Residues 206, 210, and 214 are N-ethyl-maleimide-accessible from the cytoplasmic side of the membrane and may lie on the H+ transport route. Residues 215 and 218 on TMH4, as well as residue 245 on TMH5, are Ag+-accessible but N-ethylmalcimide-inaccessible and may form part of an aqueous pocket extending from Asp(61) of subunit c to the periplasmic surface.
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