Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin

Abstract

Myoglobin (Mb) reversibly binds molecular oxygen in vertebrate muscle and consists of a polypeptide chain of 153 residues and one haem, which closely resembles one subunit of a haemoglobin (Hb) tetramer. In oxygenated myglobin (oxyMb) the iron atom is coordinated by four porphyrin nitrogen atoms, Nε of the invariant ‘proximal’ histidine (F8), and molecular… (More)
DOI: 10.1038/292081a0

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