F1 domain of ATP synthase is a rotary ATPase complex in which rotation of central γ-subunit
proceeds in 120° steps against a surrounding α3β3 fueled by ATP hydrolysis. How the ATP …

F-type ATP synthases are transmembrane enzymes, which play a central role in the
metabolism of all aerobic and photosynthetic cells and organisms, being the major source of …

The nonequilibrium coupled processes of oxidation and ATP synthesis in the biological
process of oxidative phosphorylation (OXPHOS) are fundamental to all life on our planet …

F1-ATPase is a universal multisubunit enzyme and the smallest-known motor that, fueled by
the process of ATP hydrolysis, rotates in 120o steps. A central question is how the …

Oxygen exchange reactions occurring at β-catalytic sites of the FOF1-ATP synthase/F1-
ATPase imprint a unique record of molecular events during the catalytic cycle of ATP …

The nonequilibrium coupled processes of oxidation and ATP synthesis in the fundamental
process of oxidative phosphorylation (OXPHOS) are of vital importance in biosystems …

Plasticity is a fundamental property of the neural system controlling breathing. One key
example of respiratory motor plasticity is phrenic long-term facilitation (pLTF), a persistent …

In cyanobacteria and chloroplasts (in algae and plants), ATP synthase plays a pivotal role as
a photosynthetic membrane complex responsible for producing ATP from adenosine …

Our understanding of the complex dynamic system driven by conformational change during
adenosine triphosphate (ATP) hydrolysis by F1-ATPase is of fundamental biochemical …

Vacuolar/archaeal-type ATPase (V/A-ATPase) is a rotary ATPase that shares a common
rotary catalytic mechanism with F o F 1 ATP synthase. Structural images of V/A-ATPase …