Assignment of individual metal redox states in a metalloprotein by crystallographic refinement at multiple X-ray wavelengths
Assignment of individual metal redox states in a metalloprotein by crystallographic refinement at multiple X-ray wavelengths
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DOI：
10.1021/ja067562o
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发表时间：
2007-02-28
影响因子：
15
通讯作者：
Rees, Douglas C.
中科院分区：
文献类型：
--
作者：
Einsle, Oliver;Andrade, Susana L. A.;Rees, Douglas C.
提出了一种方法，通过收集沿着相关元素的 X 射线吸收边缘传播的能量的几组衍射数据，得出蛋白质晶体内各个原子的异常散射贡献。该方法已应用于铁硫簇还原态具有局域电荷的[2Fe:2S]铁氧还蛋白模型系统。分析表明，还原后电子驻留在更靠近蛋白质表面的铁原子处。该技术对于具有非整数氧化还原态的更复杂的簇应该足够敏感，并且在晶体可用的情况下通常适用。
A method is presented to derive anomalous scattering contributions for individual atoms within a protein crystal by collecting several sets of diffraction data at energies spread along an X-ray absorption edge of the element in question. The method has been applied to a [2Fe:2S] ferredoxin model system with localized charges in the reduced state of the iron-sulfur cluster. The analysis shows that upon reduction the electron resides at the iron atom closer to the protein surface. The technique should be sufficiently sensitive for more complex clusters with noninteger redox states and is generally applicable given that crystals are available.