Energy transduction in myosin
Energy transduction in myosin
复制标题
肌球蛋白的能量转导
DOI:
10.1016/0968-0004(84)90303-7
复制
发表时间:
1984
影响因子:
13.8
通讯作者:
J. Shriver
中科院分区:
文献类型:
--
作者:
J. Shriver
It is now generally believed that the force necessary for muscle contraction results from a structural transition in the myosin crossbridge. Recent spectroscopic studies have indicated that myosin can exist in two distinct structural states. The equilibrium between the two states is poised in such a way that it can be forced in either direction with minor changes in experimental conditions. During A TP hydrolysis, myosin is forced to oscillate between the two states concomitantly with free energy dissipation. The chemical energy of A TP hydrolysis is transduced into a mechanical switching of the myosin structure between the two states. The myosin A TPase active site may be viewed as a time-dependent effector site responsible for the switching. Changes in the equilibrium between the two states have been shown to parallel changes in tension in muscle fibers. It is possible that the two myosin states may be directly correlated to the force-producing power stroke in muscle, The enzymatic coupling of vectorial processes to chemical (or photochemical) reactions is often referred to as energy transduction. Examples include pumping of H+ across a lipid bilayer as a result of a series of oxidation-reduction reactions in the respiratory chain, or the introduction of superhelices into circular DNA as a result of ATP hydrolysis by a gyrase. Energy transduction is a property of all the reactions involved (both forward and reverse) and cannot be considered a single-step process 1. However, there are events which occur in the enzyme during transduction cycles which are directly associated with the vectorial process, eg the actual movement of an ion across a membrane, or the power stroke of the myosin crossbridge during
影响因子:
2.9
作者:
Trybus,KM;Taylor,EW
通讯作者:
Taylor,EW