Abstract
The UV resonance Raman (UVRR) spectrum of oxyhemoglobin excited at 223.6 nm is dominated by bands assignable to tryptophanyl and tyrosyl residues. These vibrational modes have been employed to probe the pH dependence of structural and dynamic parameters in the protein in H 2O or D 2O buffered solutions. The effect of inositol hexaphosphate (IHP) was also investigated. We observe that, in H 2O buffered solutions, a pH increase as well as the addition of IHP leads to a general Raman intensity increase, the opposite effect being observed in D 2O buffered solutions.
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