<p> ATP synthase inhibitor prevents the enzyme from switching to ATP hydrolysis during collapse of the electrochemical gradient, for example during oxygen deprivation [<cite idref="PUB00019733"/>] ATP synthase inhibitor forms a one to one complex with the F1 ATPase, possibly by binding at the alpha-beta interface. It is thought to inhibit ATP synthesis by preventing the release of ATP [<cite idref="PUB00010058"/>]. The minimum inhibitory region for bovine inhibitor (<db_xref db="SWISSPROT" dbkey="P01096"/>) is from residues 39 to 72 [<cite idref="PUB00010058"/>]. The inhibitor has two oligomeric states, dimer (the active state) and tetramer. At low pH , the inhibitor forms a dimer via antiparallel coiled coil interactions between the C-terminal regions of two monomers. At high pH, the inhibitor forms tetramers and higher oligomers by coiled coil interactions involving the N terminus and inhibitory region, thus preventing the inhibitory activity [<cite idref="PUB00019733"/>]. </p>