| Literature DB >> 17990881 |
Toshiyuki Chatake1, Naoya Shibayama, Sam-Yong Park, Kazuo Kurihara, Taro Tamada, Ichiro Tanaka, Nobuo Niimura, Ryota Kuroki, Yukio Morimoto.
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.Entities:
Mesh:
Substances:
Year: 2007 PMID: 17990881 DOI: 10.1021/ja0749441
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419