Protonation states of buried histidine residues in human deoxyhemoglobin revealed by neutron crystallography |
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Authors: | Chatake Toshiyuki Shibayama Naoya Park Sam-Yong Kurihara Kazuo Tamada Taro Tanaka Ichiro Niimura Nobuo Kuroki Ryota Morimoto Yukio |
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Affiliation: | Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan. |
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Abstract: | 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. |
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