Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin.

Abstract

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.