NISHIZAKA Takayuki, MASAIKE Tomoko
Seibutsu Butsuri, 47(2) 118-123, 2007 Peer-reviewed
F1-ATPase is a rotary molecular motor in which unidirectional rotation of the central <symbol>γ</symbol>-subunit is powered by ATP hydrolysis in three catalytic sites arranged 120° apart around <symbol>γ</symbol>. To see how hydrolysis reactions produce mechanical rotation, we observed rotation of <symbol>γ</symbol> under the optical microscope, while watching which of the three sites bound and released a fluorescent ATP analog. The reaction scheme, including both the number of site occupancy and reactions that trigger substeps, is now established.<br>