通过中子晶体学揭示的人脱氧血红蛋白中埋藏组氨酸残基的质子化状态。
Protonation states of buried histidine residues in human deoxyhemoglobin revealed by neutron crystallography.
作者信息
Chatake Toshiyuki, Shibayama Naoya, Park Sam-Yong, Kurihara Kazuo, Tamada Taro, Tanaka Ichiro, Niimura Nobuo, Kuroki Ryota, Morimoto Yukio
机构信息
Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan.
出版信息
J Am Chem Soc. 2007 Dec 5;129(48):14840-1. doi: 10.1021/ja0749441. Epub 2007 Nov 9.
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 (Hisalpha58 and Hisbeta63) 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 alpha1beta1 hydrogen-bonding network and allow us to observe unambiguously the nature of the intradimeric interactions at an atomic level.
通过使用中子晶体学技术，明确鉴定了人脱氧血红蛋白中埋藏的组氨酸残基的质子化状态。出乎意料的是，中子结构显示α-和β-远端组氨酸（Hisα58和Hisβ63）均采用带正电荷的完全（双重）质子化形式，表明它们对玻尔效应有贡献。此外，中子数据提供了α1β1氢键网络的精确图像，并使我们能够在原子水平上明确观察二聚体内相互作用的性质。
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