Ontology highlight
ABSTRACT:
SUBMITTER: Shimo-Kon R
PROVIDER: S-EPMC2849061 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Biophysical journal 20100401 7
F(1)-ATPase is a rotary molecular motor in which the central gamma subunit rotates inside a cylinder made of alpha(3)beta(3) subunits. To clarify how ATP hydrolysis in three catalytic sites cooperate to drive rotation, we measured the site occupancy, the number of catalytic sites occupied by a nucleotide, while assessing the hydrolysis activity under identical conditions. The results show hitherto unsettled timings of ADP and phosphate releases: starting with ATP binding to a catalytic site at a ...[more]