在保存的His-X(aa) -His序列中发现的铜复合体结构和反应性
Ga Young Park1, Jung Yoon Lee, Richard A Himes
1Department of Chemistry, The Johns Hopkins University , Baltimore, Maryland 21218, United States.
Journal of the American Chemical Society
|August 30, 2014
概括
在含有histidine的铜蛋白中,陶托默的偏好显著改变了铜的含量.
科学领域:
- 生物有机化学 生物有机化学
- 协调化学 协调化学
- 蛋白质化学 蛋白质化学
背景情况:
- 氧激活的铜蛋白通常具有His-X(aa) -His合基因.
- 这些蛋白质中的伊米达环可以以分体形式存在 (δN与 εN),影响铜离子相互作用.
研究的目的:
- 为了研究胺残留的 δN 与 εN 分体偏好如何影响铜离子协调,氧化还原特性和反应性.
- 合成和表征铜(I) 复合体与 δ-HGH 和 ε-HGH 三.
主要方法:
- 在X射线吸收光谱检测中使用X射线吸收光谱.
- 密度函数理论计算密度函数理论计算
- 测量溶液导电性的测量方法
- 铜 (I) 复合物的合成和表征
主要成果:
- δ-HGH形成了一个Cu(I) 二聚合物复合物[{Cu(I) ((δ-HGH) }2](2+),而 ε-HGH形成了一个单聚合物复合物[Cu(I) ((ε-HGH) ](+).
- 单体复合物[Cu(I) ((ε-HGH) ](+) 显示出反应性,形成类似于铜单氧基酶PHM的CO添加物.
- 这种复合物还与O2和H2O2发生反应,形成新的O2附加物或Cu (II) -OOH复合物.
结论:
- 希斯蒂丁的陶托马体偏好极大地影响了生物无机系统中铜的协调几何和反应性.
- -HGH-Cu(I) 复合体作为铜单氧酶的功能模型,突出了特定协调环境的重要性.
- 这项研究提供了对铜依赖氧激活和氧化反应的机制的见解.
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