甲醇脱氢酶与其细胞色素电子受体的相互作用。
The interaction of methanol dehydrogenase and its cytochrome electron acceptor.
作者信息
Dales S L, Anthony C
机构信息
Biochemistry Department, University of Southampton, U.K.
出版信息
Biochem J. 1995 Nov 15;312 ( Pt 1)(Pt 1):261-5. doi: 10.1042/bj3120261.
Abstract
A fluorescence method is described for direct measurement of the interaction between methanol dehydrogenase (MDH) and its electron acceptor cytochrome cL. 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 cL is by way of ionic interactions between lysyl residues on its surface and carboxylate groups on the surface of cytochrome cL. 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.
摘要
本文描述了一种用于直接测量甲醇脱氢酶（MDH）与其电子受体细胞色素cL之间相互作用的荧光方法。这使得能够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。已证实初始相互作用是静电作用，但关于EDTA抑制机制的先前结论已有所修正。有人提出，MDH和细胞色素cL的初始“对接”是通过其表面的赖氨酰残基与细胞色素cL表面的羧基之间的离子相互作用实现的。这种相互作用不受EDTA抑制，我们认为EDTA的作用是通过与附近的赖氨酰残基结合，从而阻止“对接”的细胞色素移动到其进行电子转移的最佳位置，这可能涉及与MDH表面疏水通道的相互作用。
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本文引用的文献
1
Binding constants for a physiologic electron-transfer protein complex between methylamine dehydrogenase and amicyanin. Effects of ionic strength and bound copper on binding.
Biochim Biophys Acta. 1993 Aug 16;1144(1):39-45. doi: 10.1016/0005-2728(93)90028-e.
2
Binding and electron transfer reactions between methanol dehydrogenase and its physiologic electron acceptor cytochrome c-551i: a kinetic and thermodynamic analysis.
Biochemistry. 1993 Dec 28;32(51):14145-50. doi: 10.1021/bi00214a011.
3
The active site structure of the calcium-containing quinoprotein methanol dehydrogenase.含钙醌蛋白甲醇脱氢酶的活性位点结构
Biochemistry. 1993 Dec 7;32(48):12955-8. doi: 10.1021/bi00211a002.
4
Ionic strength dependence of the reaction between methanol dehydrogenase and cytochrome c-551i: evidence of conformationally coupled electron transfer.
Biochemistry. 1994 Oct 25;33(42):12600-8. doi: 10.1021/bi00208a010.
5
The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone.含吡咯喹啉醌的甲醇脱氢酶及相关醌蛋白的结构与功能。
Biochem J. 1994 Dec 15;304 ( Pt 3)(Pt 3):665-74. doi: 10.1042/bj3040665.
6
The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A.来自嗜甲基菌的醌蛋白甲醇脱氢酶在1.94埃分辨率下的精细结构。
Structure. 1995 Feb 15;3(2):177-87. doi: 10.1016/s0969-2126(01)00148-4.
7
The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27.甲醇的微生物氧化。2. 假单胞菌属M 27的甲醇氧化酶。
Biochem J. 1964 Sep;92(3):614-21. doi: 10.1042/bj0920614.
8
Bacterial oxidation of methane and methanol.甲烷和甲醇的细菌氧化作用。
Adv Microb Physiol. 1986;27:113-210. doi: 10.1016/s0065-2911(08)60305-7.
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Methods Enzymol. 1990;188:298-303. doi: 10.1016/0076-6879(90)88046-d.
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