Protonation States of Buried Histidine Residues in Human Deoxyhemoglobin Revealed by Neutron Crystallography
Journal of the American Chemical Society2007Vol. 129(48), pp. 14840–14841
Citations Over TimeTop 22% of 2007 papers
Toshiyuki Chatake, Naoya Shibayama, Sam‐Yong Park, Kazuo Kurihara, Taro Tamada, Ichiro Tanaka, Nobuo Niimura, Ryota Kuroki, Y. 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.
Related Papers
- → Terminal vs Bridging Hydrides of Diiron Dithiolates: Protonation of Fe2(dithiolate)(CO)2(PMe3)4(2012)128 cited
- → Protonation of homotroponeiron tricarbonyl and cyclooctatrienoneiron tricarbonyl complexes(1980)8 cited
- → 13C nuclear magnetic resonance study of the protonation of 2,2,4-trimethyl-1,5,9-triazacyclododecane(1988)6 cited
- → The effect of substitution on protonation sites: evidence for protonation at N(3) in N(7)-substituted adenine(1975)6 cited
- The Protonation Equili rium and Decomposition of Amino- and Hydroxyphosphonates, Phos phine Ox ides and Phosphonic Acid(2007)