Conformation of L-tyrosine studied by fluorescence-detected UV-UV and IR-UV double-resonance spectroscopy.
The laser-induced fluorescence spectrum of jet-cooled L-tyrosine exhibits more than 20 vibronic bands in the 35450-35750 cm(-1) region. We attribute these bands to eight conformers by using results of UV-UV hole-burning spectroscopy. These isomers are classified into four groups; each group consists of two rotational isomers that have a similar side-chain conformation but different orientations of the phenolic OH. The splitting of band origins of rotational isomers is 31, 21, 5, and 0 cm(-1) for these groups. IR-UV spectra suggest that conformers belonging to two of the four groups have an intramolecular OH...N hydrogen bond between the COOH and NH2 groups. By comparing experimental and theoretical results of L-tyrosine with those of L-phenylalanine, we propose probable conformers of L-tyrosine.
Inokuchi
Yoshiya
Y
Department of Chemistry, Faculty of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan.
Kobayashi
Yusuke
Y
Ito
Takafumi
T
Ebata
Takayuki
T
D003198:Computer Simulation; D004583:Electrons; D005453:Fluorescence; D008958:Models, Molecular; D008968:Molecular Conformation; D010649:Phenylalanine / Q000737:chemistry; D013057:Spectrum Analysis; D013696:Temperature; D014443:Tyrosine / Q000737:chemistry*; D014732:Vibration
D014443:Tyrosine; D010649:Phenylalanine