ATP binding rate (Kon) of ATP synthase

Value 3.6e+7 M^-1 × Sec^-1 Range: ±1000000 M^-1 × Sec^-1
Organism Bacteria Escherichia coli
Reference Ueno H, Suzuki T, Kinosita K Jr, Yoshida M. ATP-driven stepwise rotation of FoF1-ATP synthase. Proc Natl Acad Sci U S A. 2005 Feb 1 102(5):1333-8PubMed ID15668386
Method Resrearchers isolated thermophilic FoF1, which kept structural integrity in a detergent, immobilized it on a glass surface through the ß-subunits, attached a small (80 nm) bead to the c-subunit ring as a rotation probe whose viscous friction was low enough to allow full-speed rotation, and observed ATP-driven rotation with a fast (submilisecond) camera.
Comments At low ATP, ATP-waiting dwell was seen and the kon-ATP was estimated to be 3.6 x 10(7) M(-1) x s(-1). At high ATP, fast, poorly defined stepwise motions were observed that probably reflect the catalytic dwells. This value is close to that of F1 at 23°C (3.0 ± 0.1 × 10^7 M-1·s-1)
Entered by Uri M
ID 104892