Ultraviolet Raman spectroscopy indicates fast (less than 7 ns) R----T-like motion in hemoglobin.

Raman spectra of oxy- and deoxyhemoglobin obtained with 218 and 200 nm pulsed (7 ns) laser excitation show changes (loss of 880 cm-1 tryptophan band intensity, increase in the 830/850 cm-1 tyrosine doublet intensity ratio) which are attributed to the aromatic contacts (Trp beta 37-Tyr alpha 140 and Tyr alpha 42-Asp beta 99) that are specific to the T quaternary structure. At high concentration (2 mM in heme) HbCO shows the same spectral signatures as HbO2. As the HbCO concentration is decreased, however, the spectra approach those shown by deoxy-Hb. This dilution effect is attributable to photolysis, which increases with decreasing concentration. The results imply that the HbCO photoproduct shows the same aromatic environments as does deoxy-Hb. Thus, T-like contacts are apparently formed at the alpha 1 beta 2 interface within 7 ns of photolysis, a time short compared to the spectral alterations of the heme group (approximately 100 ns, approximately 1 microsecond, and approximately 20 microseconds) which have previously been attributed to tertiary and quaternary relaxations.