A 13C-NMR study of mutant hemoglobins with altered oxygen affinity.
The 13CO-NMR spectra of carbonylhemoglobins Saint Mandé (beta 102Asn----Tyr), Malmö (beta 97His----Gln), Hôtel Dieu (beta 99Asp----Gly) and Ao have been determined. The positions of the 13CO resonances for hemoglobins Ao, Malmö and Hôtel Dieu were similar indicating similar ligand environments for all. The 13CO resonance for the beta-subunit of Saint Mandé was upfield-shifted compared to the others. This is evidence that structural changes at the beta 102 position directly affect iron-ligand bonding as well as quaternary structure.
D002247:Carbon Isotopes; D002248:Carbon Monoxide; D002263:Carboxyhemoglobin; D006455:Hemoglobins, Abnormal; D006801:Humans; D009682:Magnetic Resonance Spectroscopy
D002247:Carbon Isotopes; D006455:Hemoglobins, Abnormal; C028905:hemoglobin Hotel-Dieu; C030556:hemoglobin Saint Mande; D002248:Carbon Monoxide; D002263:Carboxyhemoglobin; C041172:hemoglobin Malmo