在单分子水平上使用光致变色的 ATP 类似物可逆地控制 F(1)-ATP 酶的旋转运动。
Reversible control of F(1)-ATPase rotational motion using a photochromic ATP analog at the single molecule level.
机构信息
Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Chiyoda-Ku Tokyo 102-0076, Japan; Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259-R1-8, Midori-Ku, Yokohama 226-8503, Japan.
Research Institute for Electronic Science, Hokkaido University, N20, W10, Kita-Ku, Sapporo 001-0020, Japan.
出版信息
Biochem Biophys Res Commun. 2014 Mar 28;446(1):358-63. doi: 10.1016/j.bbrc.2014.02.117. Epub 2014 Mar 4.
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.
马达酶（如 F1-ATP 酶和驱动蛋白）利用 ATP 中的能量来驱动其运动。这些酶的分子运动对于它们的催化机制至关重要，并且使用单分子观察技术进行了彻底分析。作为分析和控制 ATP 驱动的马达酶运动的工具，我们最近合成了一种光响应的 ATP 类似物，其在核糖环的 2'位置连接了对叔丁基偶氮苯侧链。通过偶氮苯部分的顺/反异构化，我们在体外运动测定中成功地实现了对驱动蛋白-微管系统的可逆光致变色控制。在这里，我们成功地使用这种光敏 ATP 类似物控制了旋转马达酶 F1-ATP 酶的水解活性和旋转。随后的单分子观察表明，在类似物的顺式形式存在下，在 ATP 结合角度位置会出现独特的暂停。
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