Before revision:  In the presence of ionophores and uncouplers the fastest subunit rotation speeds measured in single reconstituted FoF1-ATP synthases were 180 full rounds per second , i. e. much faster than measured by biochemical ensemble averaging, but not as fast as the maximum rotational speed reported previoulsy for isolated single F1 fragments without coupling to the membrane-embedded Fo domain of the enzyme .
After revision:  In the presence of ionophores and uncouplers the fastest subunit rotation speeds measured in single reconstituted FoF1-ATP synthases were 180 full rounds per second . This was much faster than measured by biochemical ensemble averaging, but not as fast as the maximum rotational speed reported previoulsy for isolated single F1 fragments without coupling to the membrane-embedded Fo domain of the enzyme .