ATP synthase is the central enzyme for energy supply of cells. It is composed of a membrane portion (F
o) and a catalytic portion (F
1). F
1 is composed of 5 kinds of subunits (α
3β
3γδε), in which each α
1β
1 protomer has ATP-binding site. The α
3β
3 oligomer structure is needed for cooperativity of rapid ATP synthesis. Both the protomer and oligomer were reconstituted only in the case of thermophilic F
1 (TF
1). The basic structure of F
o is ab
2c
12. X-ray crystallography and nanomechanics of F
1 demonstrated the intramolecular rotation of c-γ axis, which is driven by the electrochemical potential difference of protons (ΔμH
+) across the membrane. Recent biological studies using mtDNA-less cell (ρ
0 cell) by membrane fusion, and human genetics are also described. The uncoupling proteins dissipate ΔμH
+to protect mitochondrial membrane.
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