The regulator of the F1 motor: inhibition of rotation of cyanobacterial F1ATPase by the subunit
نویسندگان
چکیده
Hiroki Konno, Tomoe Murakami-Fuse, Fumihiko Fujii, Fumie Koyama, Hanayo Ueoka-Nakanishi, Chan-Gi Pack, Masataka Kinjo and Toru Hisabori* Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, Japan, ATP System Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation (JST), Nagatsuta-cho, Midori-ku, Yokohama, Japan and Laboratory of Supramolecular Biophysics, Research Institute for Electronic Science, Hokkaido University, Kita-ku, Sapporo, Hokkaido, Japan
منابع مشابه
Inhibition of thermophilic F1-ATPase by the ε subunit takes different path from the ADP-Mg inhibition
The F1-ATPase, the soluble part of FoF1-ATP synthase, is a rotary molecular motor consisting of α3β3γδε. The γ and ε subunits rotate relative to the α3β3δ sub-complex on ATP hydrolysis by the β subunit. The ε subunit is known as an endogenous inhibitor of the ATPase activity of the F1-ATPase and is believed to function as a regulator of the ATP synthase. This inhibition by the ε subunit (ε inhi...
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