肌球蛋白ATP水解：一种涉及镁螯合物复合体的机制。
Myosin ATP hydrolysis: a mechanism involving a magnesium chelate complex.
作者信息
Burke M, Reisler E, Harrington W F
出版信息
Proc Natl Acad Sci U S A. 1973 Dec;70(12):3793-6. doi: 10.1073/pnas.70.12.3793.
Abstract
It is suggested that under physiological conditions (> 1 mM Mg(2+)) MgATP binds to myosin to form a chelate involving the two reactive sulfhydryl sites (SH(1) and SH(2)). The stability of the chelate structure results in marked inhibition of the myosin ATPase in the presence of millimolar magnesium ion. The inhibitory effect of magnesium ion can be eliminated chemically by blocking either the SH(1) or SH(2) site since this precludes formation of the chelate. In muscle, actin apparently behaves in a similar fashion in that its interaction with myosin causes a disruption of the chelate structure.
摘要
有人提出，在生理条件下（>1 mM Mg(2+)），MgATP与肌球蛋白结合形成一种螯合物，涉及两个反应性巯基位点（SH(1)和SH(2)）。螯合物结构的稳定性导致在存在毫摩尔镁离子的情况下肌球蛋白ATP酶受到显著抑制。通过阻断SH(1)或SH(2)位点，可以化学消除镁离子的抑制作用，因为这会阻止螯合物的形成。在肌肉中，肌动蛋白的行为显然类似，即它与肌球蛋白的相互作用会导致螯合物结构的破坏。
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