Transient Raman study of hemoglobin: structural dependence of the iron-histidine linkage.
Low-frequency resonance Raman spectra of transient hemoglobin species were observed within 10 nanoseconds of photolysis. The Raman frequencies of the iron-proximal histidine stretching mode for transient species having either the R or the T quaternary structure are higher than in the corresponding deoxy species. The observed frequency difference in the iron-histidine mode between the R- and T- state transients indicates that there are quaternary structure-dependent protein forces on the iron-histidine bond in the liganded hemoglobins. These differences are interpreted in terms of changes in the tilt of the histidine with respect to the heme plane.
D002263:Carboxyhemoglobin; D006418:Heme; D006454:Hemoglobins; D006639:Histidine; D006801:Humans; D007501:Iron; D009038:Motion; D009211:Myoglobin; D010782:Photolysis; D013059:Spectrum Analysis, Raman
D006454:Hemoglobins; D009211:Myoglobin; D006418:Heme; D006639:Histidine; D002263:Carboxyhemoglobin; D007501:Iron