血红蛋白中的配体结合过程。通过X射线吸收近边结构光谱研究铁的化学反应性。
Ligand binding processes in hemoglobin. Chemical reactivity of iron studied by XANES spectroscopy.
作者信息
Pin S, Valat P, Cortes R, Michalowicz A, Alpert B
出版信息
Biophys J. 1985 Dec;48(6):997-1001. doi: 10.1016/S0006-3495(85)83862-5.
Abstract
K-absorption edge of coordinated ions exhibits a fine structure (through the use of XANES, or x-ray absorption near edge structures) that reflects the electronic repartition and the chemical reactivity of these ions. Comparative analysis of iron K-absorption-edge shape for hemoglobin derivatives with different ligand affinity suggests strongly that in hemoglobin, iron-forms with high and low affinity are highly improbable.
摘要
配位离子的K吸收边呈现出一种精细结构（通过使用XANES，即X射线吸收近边结构），该结构反映了这些离子的电子分布和化学反应性。对具有不同配体亲和力的血红蛋白衍生物的铁K吸收边形状进行比较分析，强烈表明在血红蛋白中，具有高亲和力和低亲和力的铁形式极不可能存在。
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