Reversible control of F₁-ATPase rotational motion using a photochromic ATP analog at the single molecule level

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• 作者：Ei-Ichiro Sunamura^a ; ^b ; Takashi Kamei^c ; Hiroki Konno^d ; Nobuyuki Tamaoki^c ; ^{tamaoki@es.hokudai.ac.jp" class="auth_mail} ; Toru Hisabori^a ; ^b ; ^{thisabor@res.titech.ac.jp" class="auth_mail}
• 关键词：FoF1 ; FoF1-ATP synthase ; F1 (F1-ATPase) ; catalytic moiety of ATP synthase ; Fo ; membrane sector of ATP synthase ; TNP-ATP ; 2&prime ; 3&prime ; -O-(2 ; 4 ; 6-trinitrophenyl) adenosine 5&prime ; -triphosphate ; AMP-PNP ; adenylyl imidodiphosphate ; VIS light ; visible light ; ATP-AzotBu ; ATP analog containing azobenzene at the 2&prime ; position of the ribose and a tert-butyl group at the azobenzene terminus ; trans-ATP-AzotBu ; trans form of ATP-AzotBu ; cis-ATP-AzotBu ; cis form of ATP-AzotBu ; PSS ; photostationary s
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：28 March, 2014
• 年：2014
• 卷：446
• 期：1
• 页码：358-363
• 全文大小：1101 K

文摘

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鈥?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.