THE INTERACTION OF METHANOL DEHYDROGENASE AND ITS CYTOCHROME ELECTRON-ACCEPTOR
THE INTERACTION OF METHANOL DEHYDROGENASE AND ITS CYTOCHROME ELECTRON-ACCEPTOR
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DOI：
10.1042/bj3120261
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发表时间：
1995-11-15
影响因子：
4.1
通讯作者：
ANTHONY, C
中科院分区：
文献类型：
--
作者：
DALES, SL;ANTHONY, C
描述了一种直接测量甲醇脱氢酶（MDH）与其电子受体细胞色素c(L)相互作用的荧光方法。这样就可以区分影响电子转移的因素和影响初始结合或对接过程的因素。证实了初始相互作用是静电的，但先前关于EDTA抑制机制的结论已被修改。提出MDH与细胞色素c(L)的初始“对接”是通过其表面赖基残基与细胞色素c(L)表面羧酸基之间的离子相互作用实现的。这种相互作用不受EDTA的抑制，我们认为EDTA通过与附近的赖氨酸残基结合而起作用，从而阻止“停靠”的细胞色素移动到电子转移的最佳位置，这可能涉及与MDH表面的疏水漏斗的相互作用。
A fluorescence method is described for direct measurement of the interaction between methanol dehydrogenase (MDH) and its electron acceptor cytochrome c(L). This has permitted a distinction to be made between factors affecting electron transfer and those affecting the initial binding or docking process. It was confirmed that the initial interaction is electrostatic, but previous conclusions with respect to the mechanism of EDTA inhibition have been modified. It is proposed that the initial 'docking' of MDH and cytochrome c(L) is by way of ionic interactions between lysyl residues on its surface and carboxylate groups on the surface of cytochrome c(L). This interaction is not inhibited by EDTA, which we suggest acts by binding to nearby lysyl residues, thus preventing movement of the 'docked' cytochrome to its optimal position for electron transfer, which probably involves interaction with the hydrophobic funnel in the surface of MDH.