Article
Cooperation among c-subunits of FoF1-ATP synthase in rotation-coupled proton translocation.
eLife - 2 Feb 2022
Mitome Noriyo, Kubo Shintaroh, Ohta Sumie, Takashima Hikaru, Shigefuji Yuto, Niina Toru, Takada Shoji
Abstract excerpt
In FoF1-ATP synthase, proton translocation through Fo 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 FoF1-ATP synthase activity....
Topics
- Bacillus
- Bacterial Proton-Translocating ATPases
- Escherichia coli
- Molecular Dynamics Simulation
- Mutation
- Protein Conformation
- Protons