蛋白质结合和定向问题:在突变的阿苏林结合中产生偏差导电性切换
Jerry A Fereiro1, Tatyana Bendikov2, Israel Pecht3
1Department of Materials and Interfaces, Weizmann Institute of Science, Rehovot 76100, Israel.
Journal of the American Chemical Society
|November 3, 2020
概括
一种经过修改的蓝铜蛋白N42C氨酸,与野生型氨酸不同,具有可逆导电转换. 这种取决于蛋白质定向和电极结合的切换对于电子传输至关重要.
科学领域:
- 生物物理
- 分子电子
- 材料科学
背景情况:
- 蓝铜蛋白如青是重要的生物电子转移剂.
- 通过单个分子理解电子运输是分子电子学的关键.
- 蛋白质的结构和方向显著影响电荷传输特性.
研究的目的:
- 与野生类型的氨酸 (WT Az) 相比,研究改性氨酸蛋白 (N42C Az) 的电导转换行为.
- 阐明蛋白质定向和电极结合在电荷传输中的作用.
- 探索基于蛋白质的分子结合中偏差诱导导电性切换的机制.
主要方法:
- 使用N42C Az和WT Az制造固态Au-蛋白-Au分子连接.
- 作为应用偏差电压和温度的函数的导电量测量.
- 不弹性电子道光谱 (IETS) 来探测电子状态.
- 紫外光辐射光谱分析电极与蛋白质的相互作用.
主要成果:
- N42C Az显示可逆,偏差诱导电导切换在V>0.8V时几乎增加了10倍.
- 没有转换到1.2V, 之后发生了不可逆转的变化.
- 导电性是温度独立的,这表明量子力学道,并从15K转换到室温.
- 转换的差异归因于Cu (II) 协调球与电极的接近,受蛋白质定向和结合的影响.
结论:
- 蛋白质的方向和结合性质决定了分子结合中的电子传输和导电性切换.
- 与WT Az相比,N42C Az突变改变了蛋白质的方向和结合,导致不同的电性.
- 这项研究为控制生物电子设备中的电荷传输提供了基本的见解.
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