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Reversible control of F(1)-ATPase rotational motion using a photochromic ATP analog at the single molecule level.

Sunamura, Ei-Ichiro; Kamei, Takashi; Konno, Hiroki; Tamaoki, Nobuyuki; Hisabori, Toru.
Biochem Biophys Res Commun; 446(1): 358-63, 2014 Mar 28.
Artigo em Inglês | MEDLINE | ID: mdl-24607907
Motor enzymes such as F1-ATPase and kinesin utilize energy from ATP for their motion. Molecular motions of these enzymes are critical to their catalytic mechanisms and were analyzed thoroughly using a single molecule observation technique. As a tool to analyze and control the ATP-driven motor enzyme motion, we recently synthesized a photoresponsive ATP analog with a p-tert-butylazobenzene tethered to the 2' position of the ribose ring. Using cis/trans isomerization of the azobenzene moiety, we achieved a successful reversible photochromic control over a kinesin-microtubule system in an in vitro motility assay. Here we succeeded to control the hydrolytic activity and rotation of the rotary motor enzyme, F1-ATPase, using this photosensitive ATP analog. Subsequent single molecule observations indicated a unique pause occurring at the ATP binding angle position in the presence of cis form of the analog.
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