F-ATPase, also known as F-Type ATPase (also called ATP synthase), is an ATPase found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It uses a proton gradient to drive ATP synthesis by allowing the passive flux of protons across the membrane down their electrochemical gradient and using the energy released by the transport reaction to release newly formed ATP from the active site of F-ATPase. In some bacteria, sodium ions may be used instead.
F-ATPase consists of two domains:
- the Fo domain, which is integral in the membrane
- the F1, which is peripheral (on the side of the membrane that the protons are moving into).
Fo-F1 particles are mainly formed of polypeptides. The F1-particle contains 5 types of polypeptides, with the composition-ratio-- 3α:3β:1δ:1γ:1ε. The Fo has the 1a:2b:12c composition. Together they form a rotary motor. As the protons bind to the subunits of the Fo domains, they cause parts of it to rotate. This rotation is propagated by a 'camshaft' to the F1 domain. ADP and Pi (inorganic phosphate) bind spontaneously to the three β subunits of the F1 domain, so that every time it goes through a 120° rotation ATP is released (rotational catalysis).
The Bovine Mitochondrial F1-ATPase Complexed with the Inhibitor Protein If1 is commonly cited in the relevant literature. Examples of its use may be found in many cellular fundamental metabolic activities such as acidosis and alkalosis and respiratory gas exchange.
The o in the Fo stands for oligomycin, because oligomycin is able to inhibit its function.