Protonation states of buried histidine residues in human deoxyhemoglobin revealed by neutron crystallography
Protonation states of buried histidine residues in human deoxyhemoglobin revealed by neutron crystallography
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DOI：
10.1021/ja0749441
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发表时间：
2007-12-05
影响因子：
15
通讯作者：
Morimoto, Yukio
中科院分区：
文献类型：
--
作者：
Chatake, Toshiyuki;Shibayama, Naoya;Morimoto, Yukio
利用中子晶体学技术，明确地鉴定了人脱氧血红蛋白中埋藏组氨酸残基的质子化状态。出乎意料的是，中子结构揭示了α-和β-末端组氨酸（His α 58和His β 63）都采用了带正电荷的完全（双）质子化形式，这表明它们对玻尔效应的贡献。此外，中子数据提供了α（1）β（1）氢键网络的准确图像，并允许我们在原子水平上明确观察二聚体内相互作用的性质。
The protonation states of buried histidine residues in human deoxyhemoglobin were unambiguously identified by using a neutron crystallographic technique. Unexpectedly, the neutron structure reveals that both the alpha- and beta-distal histidines (His alpha 58 and His beta 63) adopt a positively charged, fully (doubly) protonated form, suggesting their contribution to the Bohr effect. In addition, the neutron data provide an accurate picture of the alpha(1)beta(1) hydrogen-bonding network and allow us to observe unambiguously the nature of the intradimeric interactions at an atomic level.