Nuclear magnetic resonance studies of hemoproteins. IV. Hindered rotation of heme side methyl group as a probe for studying van der Waals contacts in the heme side environments of myoglobin derivatives.
220 MHz roton NMR spectral evidence for restricted rotation of one methyl group in the heme side chain of ferric horse cyanomyoglobin is reported here. Temperature dependence of this methyl proton signal was computer-simulated, yielding 14,8 kcal/mol for the methyl hindered rotation. Ionic additives such as NaCl and (NH4) 2 minus SO4 caused a slackening of this restriction of methyl rotation, evidenced from collapse of methyl signal doubling by the addition of these ionic substances. This is discussed in terms of breaking of the salt bridge formed between one of the propionate COO minus group of heme and a part of the apoprotein which might lead to constraint of one of the heme side methyl groups. The peculiarity of hyperfine-shifted methyl proton signals for other myoglobin complexes such as azide and imidazole derivatives is also discussed briefly in terms of constraint of heme side methyl group buried in a hydrophobic cleft.
D000645:Ammonium Sulfate; D000818:Animals; D001386:Azides; D003486:Cyanides; D006418:Heme; D006736:Horses; D007093:Imidazoles; D007501:Iron; D009682:Magnetic Resonance Spectroscopy; D008697:Methane; D009211:Myoglobin; D011487:Protein Conformation; D012965:Sodium Chloride; D013696:Temperature; D014907:Whales
D001386:Azides; D003486:Cyanides; D007093:Imidazoles; D009211:Myoglobin; D006418:Heme; D012965:Sodium Chloride; D007501:Iron; D008697:Methane; D000645:Ammonium Sulfate