Single-molecule observation of rotation of F1-ATPase through microbeads.
Single-molecule observation of rotation of F1-ATPase through microbeads.
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通过微珠对 F1-ATPase 旋转的单分子观察。
DOI：
10.1007/978-1-59745-490-2_12
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发表时间：
2007
影响因子：
--
通讯作者：
T. Masaike
中科院分区：
文献类型：
--
作者：
T. Nishizaka;Kana Mizutani;T. Masaike
F0 F1-ATP合酶使用质子动力跨膜催化ATP的合成。F1区由5条多肽链组成，化学计量比为α3β3γδε，分离时仅将ATP水解为ADP和磷酸盐，因此称为F1-ATP酶。Paul Boyer假设F0 F1-ATP合酶中的轴结构域旋转，并最终通过直接观察证实为分离的α3β3γ亚复合物中γ亚基的旋转。ATP的一元转换诱导120°台阶，与围绕γ以120°间隔排列的三个催化位点的构型一致。我们已经通过在光学显微镜下对单个F1分子成像来显示化学和机械事件之间的关系。一个新的方案出现了：一旦催化位点与ATP结合，γ亚基总是将同一面（相互作用表面）转向承载该位点的β; ATP结合驱动γ 80°旋转;在一步之前结合ATP的位点完成水解[和/或磷酸盐释放]诱导γ 40°旋转。
F0F1-ATP synthase catalyzes the synthesis of ATP using proton-motive force across a membrane. When isolated, the F1sector, composed of five polypeptide chains with a stoichiometry of α3β3γδε, solely hydrolyzes ATP into ADP and phosphate, and is thus called F1-ATPase. Rotation of a shaft domain in F0F1-ATP synthase has been hypothesized by Paul Boyer, and ultimately was confirmed by direct observation as rotation of the γ-subunit in an isolated α3β3γ subcomplex. Unitary turnover of ATP induces 120° steps, consistent with the configuration of three catalytic sites arranged 120° apart around γ. We have shown the relationships between chemical and mechanical events by imaging individual F1molecules under an optical microscope. A new scheme emerges: as soon as a catalytic site binds ATP, the γ-subunit always turns the same face (interaction surface) to the β hosting that site; ∼80° rotation is driven by ATP binding; ∼40° rotation is induced by completion of hydrolysis [and/or phosphate release] in the site that bound ATP one step earlier.
牛线粒体 F1-ATP 酶旋转的单分子成像
DOI：
--
发表时间：
2017
期刊：
影响因子：
--
作者：
Mariel Zarco - Zavala;Duncan G.G McMillan;Suzuki Toshiharu;Hiroshi Ueno;Rikiya Watanabe;Francisco Mendoza - Hoffmann;Jose J. Garcia-Trejo;Hiroyuki Noji;Hiroshi Ueno;Hiroshi Ueno;Hiroshi Ueno
通讯作者：
Hiroshi Ueno
影响因子：
11.4
作者：
Tominaga, M;Kojima, H;Oiwa, K
通讯作者：
Oiwa, K