||Bacteria Escherichia coli
||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
||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.
||The rotation rates at various ATP concentrations obeyed the curve defined by a Km of approximately 30 microM and a Vmax of approximately 350 revolutions per second (at 37 degrees C).