ATP合酶（F0F1）中c亚基寡聚体的机械旋转：直接观察

Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation.

作者信息

Sambongi Y, Iko Y, Tanabe M, Omote H, Iwamoto-Kihara A, Ueda I, Yanagida T, Wada Y, Futai M

机构信息

Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, CREST (Core Research for Evolutional Science and Technology) of Japan Science and Technology Corporation, Ibaraki, Osaka 567-0047, Japan.

出版信息

Science. 1999 Nov 26;286(5445):1722-4. doi: 10.1126/science.286.5445.1722.

DOI:10.1126/science.286.5445.1722

PMID:10576736

Abstract

F0F1, found in mitochondria or bacterial membranes, synthesizes adenosine 5'-triphosphate (ATP) coupling with an electrochemical proton gradient and also reversibly hydrolyzes ATP to form the gradient. An actin filament connected to a c subunit oligomer of F0 was able to rotate by using the energy of ATP hydrolysis. The rotary torque produced by the c subunit oligomer reached about 40 piconewton-nanometers, which is similar to that generated by the gamma subunit in the F1 motor. These results suggest that the gamma and c subunits rotate together during ATP hydrolysis and synthesis. Thus, coupled rotation may be essential for energy coupling between proton transport through F0 and ATP hydrolysis or synthesis in F1.

摘要

存在于线粒体或细菌膜中的F0F1，通过与电化学质子梯度偶联来合成腺苷5'-三磷酸（ATP），并且还能使ATP可逆水解以形成该梯度。连接到F0的c亚基寡聚体的肌动蛋白丝能够利用ATP水解的能量进行旋转。c亚基寡聚体产生的旋转扭矩达到约40皮牛-纳米，这与F1马达中γ亚基产生的扭矩相似。这些结果表明，在ATP水解和合成过程中，γ亚基和c亚基一起旋转。因此，耦合旋转对于通过F0的质子运输与F1中的ATP水解或合成之间的能量耦合可能至关重要。