Publications by authors named "Yuto Shigefuji"
Article Synopsis
- In FF-ATP synthase, the rotation of the -subunit oligomeric ring is driven by proton movement through the F-subunit, and key glutamic acid residues play a role in proton uptake and release.
- Recent experiments with PS3 ATP synthase, containing a mutated -ring, showed that mutations at specific glutamic acid sites diminished ATP synthesis and proton pump activities, indicating that these -subunits work cooperatively.
- Simulations further supported these findings by revealing that proton uptake in mutated -subunits is shared between them, which aligns with the observed cooperative behavior in the biochemical assays.
