Eisenberg E, Hill T L
Science. 1985 Mar 1;227(4690):999-1006. doi: 10.1126/science.3156404.
Muscle contraction occurs when the actin and myosin filaments in muscle are driven past each other by a cyclic interaction of adenosine triphosphate (ATP) and actin with cross-bridges that extend from myosin. Current biochemical studies suggest that, during each adenosine triphosphatase cycle, the myosin cross-bridge alternates between two main conformations, which differ markedly in their strength of binding to actin and in their overall structure. Binding of ATP to the cross-bridge induces the weak-binding conformation, whereas inorganic phosphate release returns the cross-bridge to the strong-binding conformation. This cross-bridge cycle is similar to the kinetic cycle that drives active transport and illustrates the general principles of free energy transduction by adenosine triphosphatase systems.
当肌肉中的肌动蛋白丝和肌球蛋白丝通过三磷酸腺苷(ATP)与肌动蛋白的循环相互作用以及从肌球蛋白延伸出的横桥而相互滑过时,肌肉收缩就会发生。目前的生化研究表明,在每个三磷酸腺苷酶循环中,肌球蛋白横桥在两种主要构象之间交替,这两种构象在与肌动蛋白结合的强度和整体结构上有显著差异。ATP与横桥的结合诱导弱结合构象,而无机磷酸的释放使横桥恢复到强结合构象。这种横桥循环类似于驱动主动运输的动力学循环,并说明了三磷酸腺苷酶系统自由能转导的一般原理。