Oosawa Fumio
Aichi Institute of Technology, Research Institute for Industrial Technology, Yagusa-cho, Yachigusa 1247, Aichi, Toyota 470-0392, Japan.
Biochem Biophys Res Commun. 2008 Apr 25;369(1):144-8. doi: 10.1016/j.bbrc.2007.11.186. Epub 2007 Dec 26.
Various myosin-actin systems do not always show the same sliding behaviors. To make the situation clear, discussions are concentrated on the unit event of sliding of the chemo-mechanical enzyme composed of a single myosin head and a single actin filament with regulatory proteins. The popular idea of the one-to-one correspondence between the chemical state and the physical state or between the chemical reaction step and the physical conformational change is reexamined. It is likely that the sites and the modes of interaction between myosin head and actin filament during the ATP hydrolysis are more multiple and variable, and the input-output coupling in the chemo-mechanical enzyme is loose.
各种肌球蛋白 - 肌动蛋白系统并不总是表现出相同的滑动行为。为了弄清楚这种情况,讨论集中在由单个肌球蛋白头部、单个肌动蛋白丝以及调节蛋白组成的化学 - 机械酶的滑动单元事件上。重新审视了化学状态与物理状态之间或化学反应步骤与物理构象变化之间一一对应的流行观点。在ATP水解过程中,肌球蛋白头部与肌动蛋白丝之间的相互作用位点和模式可能更多样且可变,并且化学 - 机械酶中的输入 - 输出耦合是松散的。