Correlation between quaternary structure and ligand dissociation kinetics for fully liganded hemoglobin.
The quaternary structures of fully liganded adult hemoglobin and hemoglobin Kansas (alpha2beta2 102 Asn-thr) bound by carbon monoxide or nitric oxide were spectroscopically characterized using high-resolution nuclear magnetic resonance (NMR) and ultraviolet circular dichroism (CD). The spectral markers used for the quarternary transition were the line in the NMR spectrum in H2O-14 ppm downfield from 2,2-dimethyl-2-silapentane-5-sulfonate and the negative peak at 285 nm in the ultraviolet CD spectrum. In the nitrosyl derivatives, these two structural markers were compared with the electron paramagnetic resonance (EPR) spectrum at room temperature for the purpose of correlating structural changes in the protein with changes at the heme...
D001665:Binding Sites; D002248:Carbon Monoxide; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D006801:Humans; D007294:Inositol / Q000031:analogs & derivatives*; D007615:Kansas; D007700:Kinetics; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D009569:Nitric Oxide; D010833:Phytic Acid; D011485:Protein Binding; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013997:Time Factors
D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D008024:Ligands; D009569:Nitric Oxide; D007294:Inositol; D010833:Phytic Acid; D002248:Carbon Monoxide