Format

Send to

Choose Destination
Biophys J. 2004 Oct;87(4):2148-63.

Torque generation by the Fo motor of the sodium ATPase.

Author information

1
Department of Molecular Biology, Policy and Management, University of California, Berkeley, California 94720-3112, USA.

Abstract

Based on recent structural and functional findings, we have constructed a mathematical model for the sodium-driven Fo motor of the F1Fo-ATPase from the anaerobic bacterium Propionigenium modestum. The model reveals the mechanochemical principles underlying the Fo motor's operation, and explains all of the existing experimental data on wild-type and mutant Fo motors. In particular, the model predicts a nonmonotonic dependence of the ATP hydrolysis activity on the sodium concentration, a prediction confirmed by new experiments. To explain experimental observations, the positively charged stator residue (R227) must assume different positions in the ATP synthesis and hydrolysis directions. This work also illustrates how to extract a motor mechanism from dynamical experimental observations in the absence of complete structural information.

PMID:
15454418
PMCID:
PMC1304641
DOI:
10.1529/biophysj.104.042093
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center