Single Molecule Behavior of Inhibited and Active States ofEscherichia coliATP Synthase F1Rotation

Roles of the β subunit hinge domain in ATP synthase F1 sector: Hydrophobic network formed by introduced βPhe174 inhibits subunit rotation

(2010) Mayumi Nakanishi-Matsui et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

The mechanism of rotating proton pumping ATPases

(2010) Mayumi Nakanishi-Matsui et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS

36° step size of proton-driven c-ring rotation in FoF1-ATP synthase

(2009) Monika G Düser et al.   EMBO JOURNAL

Effect of ε subunit on the rotation of thermophilicBacillusF1-ATPase

(2009) Masato Tsumuraya et al.   FEBS LETTERS

Temperature Dependence of Single Molecule Rotation of the Escherichia coli ATP Synthase F1Sector Reveals the Importance of γ-β Subunit Interactions in the Catalytic Dwell

(2009) Mizuki Sekiya et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The rotary mechanism of the ATP synthase

(2008) Robert K. Nakamoto et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

A Rotor-Stator Cross-link in the F1-ATPase Blocks the Rate-limiting Step of Rotational Catalysis

(2008) Joanne A. Baylis Scanlon et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation

(2008) D. Okuno et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Effects of mutations in the β subunit hinge domain on ATP synthase F1 sector rotation: Interaction between Ser 174 and Ile 163

(2007) Sachiko Kashiwagi et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS