Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin.
Hemoglobin M Milwaukee (beta 67E11 val leads to Glu) is a naturally occurring valency hybrid containing two permanently oxidized hemes in the beta-chains. In this mutant, the two abnormal beta-chains cannot combine with oxygen, whereas the two alpha-chains are normal and can combine with oxygen cooperatively with a Hill coefficient of approximately 1.3. High-resolution proton nuclear magnetic resonance spectroscopy at 250 MHz has been used to investigate the hyperfine shifted resonances of the abnormal ferric beta-chains of Hb M Milwaukee over the spectral region from -30 to -60 parts per million from water at pD 7 and 30 degrees.
D000494:Allosteric Regulation; D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006418:Heme; D006455:Hemoglobins, Abnormal / Q000378:metabolism; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D010100:Oxygen / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014922:Wisconsin
D006455:Hemoglobins, Abnormal; D008024:Ligands; D006418:Heme; D010100:Oxygen