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The nitro stretch as a probe of the environment of nitrophenols and nitrotyrosines
Author(s) -
Quaroni L.,
Smith W. E.
Publication year - 1999
Publication title -
journal of raman spectroscopy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.748
H-Index - 110
eISSN - 1097-4555
pISSN - 0377-0486
DOI - 10.1002/(sici)1097-4555(199907)30:7<537::aid-jrs414>3.0.co;2-b
Subject(s) - nitro , chemistry , hydrogen bond , intramolecular force , intermolecular force , raman spectroscopy , molecule , raman scattering , nitrophenol , hydrogen , nitro compound , residue (chemistry) , crystallography , stereochemistry , photochemistry , organic chemistry , optics , alkyl , physics , catalysis
Raman scattering is a sensitive and selective probe of the environment of nitro groups in nitrated proteins. As a model study to aid the interpretation of the changes observed, the spectra of 2‐nitrophenol in solvents with different hydrogen bonding characteristics were recorded. An intramolecularly hydrogen‐bonded and an intermolecularly hydrogen‐bonded form of the molecule were identified from the wavenumber and intensity of the symmetric stretching vibration of the nitro group. In addition, the wavenumber of the mode is sensitive to the strength of the hydrogen‐bonding interactions. The application of the conclusions to two nitrated proteins shows that in one case where the nitro group is on the surface intermolecular hydrogen bonding occurs, whereas in the other where the nitro groups is on an internal residue intramolecular hydrogen bonding occurs. Copyright © 1999 John Wiley & Sons, Ltd.