Cooperation among c-subunits of F_oF₁-ATP synthase in rotation-coupled proton translocation.

ABSTRACT: In F_oF₁-ATP synthase, proton translocation through F_o drives rotation of the c-subunit oligomeric ring relative to the a-subunit. Recent studies suggest that in each step of the rotation, key glutamic acid residues in different c-subunits contribute to proton release to and proton uptake from the a-subunit. However, no studies have demonstrated cooperativity among c-subunits toward F_oF₁-ATP synthase activity. Here, we addressed this using Bacillus PS3 ATP synthase harboring a c-ring with various combinations of wild-type and cE56D, enabled by genetically fused single-chain c-ring. ATP synthesis and proton pump activities were decreased by a single cE56D mutation and

SUBMITTER: Mitome N 

PROVIDER: S-EPMC8809890 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature