人类朊蛋白的一个八肽重复扩展改变了八肽重复结构域内的 Zn2+和 Cu2+配位环境。
One octarepeate expansion to the human prion protein alters both the Zn2+ and Cu2+ coordination environments within the octarepeate domain.
机构信息
Department of Chemistry/216, University of Nevada, Reno, Reno, Nevada 89557, United States.
出版信息
Inorg Chem. 2011 Feb 21;50(4):1173-5. doi: 10.1021/ic102294u. Epub 2011 Jan 20.
Abstract
The influence of a single octarepeat expansion on the Cu(II) and Zn(II) coordination environments within the octarepeat domain of the human prion protein is examined. Using X-ray absorption spectroscopy and diethyl pyrocarbonate labeling studies, we find that at low copper concentrations the "normal" octarepeat domain (four PHGGGWGQ repeats) coordinates Zn(II) in an (N/O)(6) coordination environment with two histidine residues and Cu(II) in a redox-inactive (N/O)(4) coordination environment using one imidazole residue. Expansion of the octarepeat region by one repeat (five PHGGGWGQ repeats) yields a three-histidine (N/O)(6) coordination environment for Zn(II) and a two-histidine (N/O)(4) coordination environment for Cu(II) at low copper concentrations. This Cu(II)[(N/O)(2)-histidine(2)] coordination motif is redox-active and capable of generating H(2)O(2) under reducing aerobic conditions.
摘要
研究了人类朊蛋白八肽重复区单个八重复扩展对 Cu(II)和 Zn(II)配位环境的影响。利用 X 射线吸收光谱和二乙基焦碳酸盐标记研究，我们发现，在低铜浓度下，“正常”八肽重复区（四个 PHGGGWGQ 重复）以（N/O）（6）配位环境与 Zn(II)配位，其中两个组氨酸残基和 Cu(II)以氧化还原非活性（N/O）（4）配位环境与一个咪唑残基配位。八肽重复区扩展一个重复（五个 PHGGGWGQ 重复）导致 Zn(II)的三组氨酸（N/O）（6）配位环境和 Cu(II)的二组氨酸（N/O）（4）配位环境在低铜浓度下。这种 Cu(II)[(N/O)(2)-组氨酸(2)]配位基元是氧化还原活性的，并且能够在还原需氧条件下生成 H(2)O(2)。
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