English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance ATP synthase produces most of the ATP in respiratory and photosynthetic cells. It is a rotary motor enzyme and its catalytic portion F1 -ATPase hydrolyzes ATP to drive rotation of the central γ subunit. Efficiency of chemomechanical energy conversion by this motor is always near-perfect under different ATP hydrolysis energy (ΔG ATP ) conditions. However, the mechanism for the efficient conversion remains unknown. We measured the torque as a function of rotation angle under different ΔG ATP conditions and estimated mechanical work. The torque profiles show three sawtooth-like repeats during a single ATP hydrolysis. When concentrations of ATP/ADP and Pi in the environment are changed, the height, and hence the area, of the sawtooth changes accordingly so that mechanical work can always match ΔG ATP .

Simple mechanism whereby the F 1 -ATPase motor rotates with near-perfect chemomechanical energy conversion

Simple mechanism whereby the F ₁ -ATPase motor rotates with near-perfect chemomechanical energy conversion