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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >The binding of cytochrome c to neuroglobin: A docking and surface plasmon resonance study
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The binding of cytochrome c to neuroglobin: A docking and surface plasmon resonance study

机译：细胞色素c与神经球蛋白的结合：对接和表面等离子体共振研究

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摘要

It has recently been proposed that the role of neuroglobin in the protection of neurons from ischaemia induced cell death requires the formation of a transient complex with cytochrome c. No such complex has yet been isolated. Here, we present the results of soft docking calculations, which indicate one major binding site for cytochrome c to neuroglobin. The results yield a plausible structure for the most likely complex structure in which the hemes of each protein are in close contact. NMR analysis identifies the formation of a weak complex in which the heme group of cytochrome c is involved. surface plasmon resonance studies provide a value of 45 mu M for the equilibrium constant for cytochrome c binding to neuroglobin, which increases significantly as the ionic strength of the solution increases. The temperature dependence of the binding constant indicates that the complex formation is associated with a small unfavourable enthalpy change (1.9 kcal mol(-1)) and a moderately large, favourable entropy change (14.8 cal mol(-1) deg(-1)). The sensitivity of the binding constant to the presence of salt suggests that the complex formation involves electrostatic interactions. (C) 2008 Elsevier B.V. All rights reserved.
机译：最近有人提出，神经球蛋白在保护神经元免受缺血引起的细胞死亡中的作用需要与细胞色素c形成瞬时复合物。还没有分离出这样的复合物。在这里，我们介绍了软对接计算的结果，该结果表明了细胞色素c与神经球蛋白的一个主要结合位点。结果为最可能的复杂结构提供了一个合理的结构，其中每种蛋白质的血红素紧密接触。 NMR分析确定了弱复合物的形成，其中涉及细胞色素c的血红素基团。表面等离振子共振研究提供了45μM的值，用于细胞色素c结合神经球蛋白的平衡常数，随着溶液离子强度的增加而显着增加。结合常数的温度依赖性表明复合物的形成与较小的焓变（1.9 kcal mol（-1））和适度较大的有利熵变（14.8 cal mol（-1）deg（-1）相关）。结合常数对盐的存在的敏感性表明，络合物的形成涉及静电相互作用。 （C）2008 Elsevier B.V.保留所有权利。

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