EPR characterization of alcohol complexes of ferric myoglobin and hemoglobin.
Frozen solution electron paramagnetic resonance spectra of the aquo, methanol, and ethanol complexes of ferric myoglobin and hemoglobin are quantitatively analyzed in terms of the rhombic to tetragonal symmetry ratio and the admixture of quartet states, both with regard to central values of these parameters and the widths of their distributions. In both the methanol and ethanol complexes of ferric myoglobin the main change from the aquo complex is a narrowing of the spread in the rhombic to tetragonal symmetry ratio (reduction in structural variation). The alcohol complexes of both the alpha- and beta-chains within the tetramer of ferric hemoglobin are characterized by a lowering of symmetry (as compared with the aquo complex). Qualitative differences in distribution widths among the complexes are consistent with an origin in molecular structure and dynamics rather than in ice matrix-induced strain.
D000818:Animals; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D000431:Ethanol / Q000378:metabolism*; D006420:Hemeproteins / Q000378:metabolism*; D006736:Horses; D006801:Humans; D007700:Kinetics; D008706:Methemoglobin / Q000378:metabolism*; D008786:Metmyoglobin / Q000378:metabolism*; D011485:Protein Binding; D014907:Whales
D006420:Hemeproteins; D008786:Metmyoglobin; D000431:Ethanol; D008706:Methemoglobin