Optical absorption spectra of deoxy- and oxyhemoglobin in the temperature range 300-20 K. Relation with protein dynamics.
We have studied the optical absorption spectra of human deoxy- and oxyhemoglobin in the temperature range 300-20 K and in the wavelength range 350-1350 nm. By lowering the temperature, a narrowing and a shift of all bands were observed together with a sizeable increase of the integrated intensities of the charge-transfer bands of deoxyhemoglobin. At all temperatures the spectra are in full agreement with the band assignment previously suggested in the literature and no new relevant bands have been detected for both deoxy- and oxyhemoglobin. Analysis of the first and second moment of the bands, within the framework of the harmonic Franck-Condon approximation, gave information on the dynamic properties of the heme in the heme pocket.
D005615:Freezing; D006454:Hemoglobins / Q000378:metabolism*; D010108:Oxyhemoglobins / Q000378:metabolism*; D011487:Protein Conformation; D013053:Spectrophotometry
D006454:Hemoglobins; D010108:Oxyhemoglobins