Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 66; no. 11; pp. 1144 - 1152
• Main Authors: Kovalevsky, Andrey, Chatake, Toshiyuki, Shibayama, Naoya, Park, Sam-Yong, Ishikawa, Takuya, Mustyakimov, Marat, Fisher, S. Zoe, Langan, Paul, Morimoto, Yukio
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.11.2010
• Subjects: Adult; AFFINITY; Bohr effect; CHAINS; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLOGRAPHY; deoxy form; deuterated water; Hemoglobin; Hemoglobins - chemistry; Hemoglobins - metabolism; HISTIDINE; Histidine - chemistry; Histidine - metabolism; Human; human hemoglobin; Humans; INTERACTIONS; INTERFACES; Models, Molecular; NEUTRON DIFFRACTION; neutron protein crystallography; NEUTRONS; OXYGEN; Oxygen - chemistry; Protein Conformation; Protein Subunits; Proteins; Protonation; protonation states; PROTONS; Research Papers; Residues; STABILITY

The protonation states of the histidine residues key to the function of deoxy (T‐state) human hemoglobin have been investigated using neutron protein crystallography. These residues can reversibly bind protons, thereby regulating the oxygen affinity of hemoglobin. By examining the OMIT Fo − Fc and 2...