Hydrophobic interactions in metalloporphyrin-peptide complexes
Hydrophobic interactions in metalloporphyrin-peptide complexes
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DOI：
10.1021/ic990405o
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发表时间：
2000-11-27
影响因子：
4.6
通讯作者：
Suslick, KS
中科院分区：
文献类型：
--
作者：
Huffman, DL;Suslick, KS
在水溶液中合成了血红素−低聚铁配合物，并用分光光度滴定法测定了它们的平衡生成常数。配位组氨酸两侧的疏水残基的存在极大地增加了多肽与血红素的结合超过20kJ/mol。
Synthetic heme−oligopeptide complexes of coproporphyrin-I-atoiron(III) have been prepared in aqueous solution, and their equilibrium formation constants have been determined by spectrophotometric titration. The presence of hydrophobic residues flanking the coordinated histidine dramatically increase peptide binding to the heme by more than 20 kJ/mol.