Stuhrmann H B, Notbohm H
Proc Natl Acad Sci U S A. 1981 Oct;78(10):6216-20. doi: 10.1073/pnas.78.10.6216.
The anomalous dispersion of iron at its K-absorption edge in small-angle scattering of an aqueous solution of hemoglobin has been used to establish the geometrical arrangement of the four iron atoms in this protein. Although the anomalous contributions are 0.001-0.01 of the total scattering, experiments with synchrotron radiation from the storage ring DORIS have shown that these effects can be measured with an average precision of approximately 10% at each of the 50 points of the scattering curve. The anomalous scattering represents the convolution of the whole structure with the configuration of the four iron atoms of hemoglobin. Analysis in terms of multipoles suggests that tetrahedral symmetry of both the subunit arrangement and the iron structure is a dominant feature. The mean distance between the iron atoms of 26 A derived from this experiment compares well with that derived from crystallographic data.
血红蛋白水溶液小角散射中铁在其K吸收边的反常色散已被用于确定该蛋白质中四个铁原子的几何排列。尽管反常贡献仅占总散射的0.001 - 0.01，但利用来自储存环DORIS的同步辐射进行的实验表明，在散射曲线的50个点中的每一点上，这些效应都能以约10%的平均精度被测量。反常散射代表了整个结构与血红蛋白四个铁原子构型的卷积。基于多极子的分析表明，亚基排列和铁结构的四面体对称性是一个主要特征。从该实验得出的铁原子间平均距离为26 Å，与从晶体学数据得出的结果相当吻合。
