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UV resonance raman spectroscopy of the aromatic residues in oxyhemoglobin

✍ Scribed by Saïd El Antri; Olivier Sire; Bernard Alpert; Pierre-Yves Turpin; Laurent Chinsky

Publisher
Elsevier Science
Year
1989
Tongue
English
Weight
461 KB
Volume
164
Category
Article
ISSN
0009-2614

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✦ Synopsis

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 Hz0 or DZO buffered solutions. The effect of inositol hexaphosphate (IHP) was also investigated. We observe that, in Hz0 buffered solutions, a pH increase aswell as the addition of IHP leads to a general Raman intensity increase, the opposite effect being observed in D,O buffered solutions.

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