Markin V S, Liu D, Gimsa J, Strobel R, Rosenberg M D, Tsong T Y
Department of Biochemistry, University of Minnesota College of Biological Sciences, St. Paul 55108.
J Membr Biol. 1992 Mar;126(2):137-45. doi: 10.1007/BF00231912.
To explain the electrical activation of several membrane ATPases, an electroconformational coupling (ECC) model has previously been proposed. The model explained many features of experimental data but failed to reproduce a window of the field intensity for the stimulated activity. It is shown here that if the affinities of the ion for the two conformational states of the transporter (one with binding site on the left side and the other on the right side of the membrane) are dependent on the electric field, the field-dependent transport can exhibit the observed window. The transporter may be described as a channel enzyme which opens to one side of the membrane at a time. It retains the energy-transducing ability of the earlier ECC models. Analysis of the channel enzyme in terms of the Michaelis-Menten kinetics has been done. The model reproduced the amplitude window for the electric field-induced cation pumping by (Na,K)-ATPase.
为了解释几种膜ATP酶的电激活过程,此前已提出一种电构象偶联(ECC)模型。该模型解释了实验数据的许多特征,但未能重现刺激活性的场强窗口。本文表明,如果离子对转运体两种构象状态(一种在膜左侧有结合位点,另一种在膜右侧有结合位点)的亲和力取决于电场,那么场依赖转运就可以呈现出观察到的窗口。转运体可被描述为一种通道酶,它一次向膜的一侧开放。它保留了早期ECC模型的能量转换能力。已根据米氏动力学对通道酶进行了分析。该模型重现了电场诱导(Na,K)-ATP酶阳离子泵浦的幅度窗口。