Characterization of transferrin metal-binding sites by diffusion-enhanced energy transfer.
Characterization of transferrin metal-binding sites by diffusion-enhanced energy transfer.
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通过扩散增强能量转移表征转铁蛋白金属结合位点。
DOI：
10.1021/bi00563a019
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发表时间：
1980
期刊：
影响因子：
2.9
通讯作者：
Meares,CF
中科院分区：
文献类型：
--
作者：
Yeh,SM;Meares,CF
Simon M. Yeh 和 Claude F. Meares* 摘要：通过测量从水溶液中自由扩散的铽螯合物到与转铁蛋白结合的金属离子的能量转移，估算了从蛋白质表面到人血清转铁蛋白的两个特定金属结合位点中的铁或锰离子的距离。此外，还研究了蛋白质的两种单铁形式，以及使用草酸盐代替碳酸氢盐作为铁 (III) 与转铁蛋白结合的辅助阴离子形成的二铁复合物。电中性铽 (III)-iV-(2-羟基-乙基)乙二胺三乙酸盐与 FeA、FeB 和 Fe2 形式的转铁蛋白之间能量转移的二级速率常数为 0.9 X 105 M'1 s'1, 1.4 X 105 M'1
Simon M. Yeh and Claude F. Meares* abstract: The distance from the protein surface to ferric or manganic ions in the two specific metal-binding sites of human serum transferrin has been estimated by measuring energy transfer from freely diffusing terbium chelates in aqueous solution to transferrin-bound metal ions. In addition, both monoferric forms of the protein were studied, as well as the diferric complex formed by using oxalate instead of (bi-carbonate as the auxiliary anion in binding of iron (III) to transferrin. Second-order rate constants for energy transfer between electrically neutral terbium (III)-iV-(2-hydroxy-ethyl) ethylenediaminetriacetate and the FeA, FeB, and Fe2 forms of transferrin were 0.9 X 105 M'1 s'1, 1.4 X 105 M'1