| Research Abstract |
Major results are as follows.
1)A regulatory subunit, ε, binds ATP and it changes its conformation depending on the protonic electrochemical potential difference across the membrane.
2)By introducing Trp residue into the vicinity of the catalytic site on β subunits, we could clarify the origin of apparent negative cooperativity.
3)ATP binding per se drives 80 degree step motion before hydrolysis on the enzyme.
4)By using fluorescent ATP analogue, we could directly observe ATP binding and rotation simultaneously We found that once ATP binds, it remains bound until γ subunit rotates 240 degree.
5)By using magnetic beads and forcing F_1-ATPase to rotate in synthetic direction, we could show continuous ATP synthesis.
|
