Abstract
Among other methods1, resonance Raman spectroscopy is a particularly useful technique for the study of haem proteins because it monitors conf ormational changes that are reflected in vibrational degrees of freedom of the haem moiety. Its application to haemoglobin (Hb)2–7 has recently been extended by the development of time-resolved techniques. High frequency bands in time-resolved resonance Raman (TR3) spectra obtained with excitation into the α, β absorption bands have already been used to study the conformational changes of the haem associated with the photolytic removal of CO from carboxyhaemoglobin (HbCO) at 30 ps and 20 ns (ref. 7). We report here TR3 spectra, obtained by excitation into the Soret absorption band, containing low-frequency bands which provide a detailed characterization of the Hb conformation formed within 8 ns of the photolysis of HbCO.
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Irwin, M., Atkinson, G. Low-frequency resonance Raman spectroscopy of the deoxyhaemoglobin transient of photolysed carboxyhaemoglobin. Nature 293, 317–318 (1981). https://doi.org/10.1038/293317a0
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DOI: https://doi.org/10.1038/293317a0
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