Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin
Phillips, S.E.; Schoenborn, B.P.
Nature 292(5818): 81-82
1981
ISSN/ISBN: 0028-0836 PMID: 7278969 Document Number: 178573
In oxygenated myoglobin the O2 molecule lies in a tight pocket, bounded by 2 hydrophobic groups (Phe CD1 Val E11) and the side chain of the distal histidine (E7). The function of the residue is not clear, although it does present steric hindrance to linear ligands such as CO and favors bent ones, such as O2. The imidazole stabilizes bound O2 with a H bond, as revealed by neutron diffraction analysis of sperm whale myoglobin.