It has been proposed that during ATP synthesis/hydrolysis F1 ATPases experience a complex pattern of nucleotide binding and release during the catalytic cycle (binding change mechanism). This type of mechanism has implications that can be correlated with the structure of the enzyme. F1-ATPases (stoichiometry α3β3γδε) are essentially a symmetrical trimer of pairs of the major subunits (α and β); the minor subunits (γ, δ and ε) are in single copies and interact with the trimer in an asymmetrical fashion. The asymmetry introduced by the minor subunits has important structural and functional consequences: (1) it introduces differences between the potentially equivalent binding and catalytic sites in the major subunits, (2) it restricts the ways in which a binding change mechanism can occur, and (3) it governs the way in which the F1 interacts with the (asymmetrical) F0 sector.
|Original language||English (US)|
|Number of pages||5|
|Journal||Journal of Bioenergetics and Biomembranes|
|State||Published - Oct 1992|
ASJC Scopus subject areas
- Cell Biology