Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures.
Resonance Raman spectra have been obtained of the alpha deoxy and beta deoxy subunits within valency hybrid hemoglobins both in the high-affinity (R) and low-affinity (T) structures. Upon conversion from the R to the T structure, the vibrational frequency of the Fe(II)-N epsilon(His-F8) bond changes from 223 to 207 or 203 cm-1 in the alpha deoxy subunit and from 224 to 220 or 217 cm-1 in the beta deoxy subunit. We estimate that the Fe(II)-N epsilon(His-F8) bond is stretched by the R leads to T transition 3 times more in the alpha subunit (0.024 A) than in the beta subunit (0.0085 A) and, accordingly, the strain energy developed in that bond is 8 times larger in the alpha than in the beta subunit. Hence, the oxygen affinity of the alpha and beta subunits may be regulated by different mechanisms.
D000494:Allosteric Regulation; D005296:Ferrous Compounds; D006418:Heme; D006441:Hemoglobin A; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D006639:Histidine; D046911:Macromolecular Substances; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman
D005296:Ferrous Compounds; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D046911:Macromolecular Substances; D006418:Heme; D006639:Histidine; D006441:Hemoglobin A