Heme orientational heterogeneity in deuterohemin-reconstituted horse and human hemoglobin characterized by proton nuclear magnetic resonance spectroscopy.
The number of 2,4-H signals of met-cyano and deoxy deuteroheme-reconstituted sperm whale Mb are shown to reflect the known degree of heme rotational disorder in this modified protein. Using these unique spectral windows for the 2,4-H signals, we show that both horse and human Hb reconstituted with deuteroheme exhibit significant molecular heterogeneity which is consistent with approximately 20% heme rotational disorder within each subunit.
D000818:Animals; D006418:Heme / Q000031:analogs & derivatives / Q000032:analysis*; D006427:Hemin / Q000031:analogs & derivatives; D006441:Hemoglobin A; D006736:Horses; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D013045:Species Specificity
C011219:deuterohemin; D006418:Heme; D006427:Hemin; D006441:Hemoglobin A