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The protein dynamics of human hemoglobin following ligand photolysis was studied by time-resolved resonance Raman spectroscopy. The time-resolved spectra of two kinds of recombinant hemoglobin expressed in Escherichia coli, normal recombinant hemoglobin and the α(V1M)/β(V1M) double mutant, were compared with those of human adult hemoglobin (HbA) purified from blood. A frequency shift of the iron–histidine...
Time-resolved resonance Raman spectroscopy on human adult hemoglobin (HbA) following ligand photolysis revealed that the frequency of the iron–histidine stretching [ν(Fe–His)] mode exhibited a 2-cm −1 downshift with a time constant of about 300ps, suggesting a structural change in the heme pocket following the ligand photolysis. Low-frequency heme modes suggested that the primary metastable...
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