Photostability of amino acids: photodissociation dynamics  of phenylalanine chromophores.
The theoretical prediction of H atom elimination on the excited state of phenol, imidazole and indole, the respective chromophores for the amino acids tyrosine, histidine and tryptophan, and the confirmation of theoretical prediction by experimental observations have a great impact on the explanation of photostability of amino acids upon irradiation with UV photons. On the other hand, no theoretical prediction of the excited state photodissociation dynamics has been made on the other aromatic amino acid, phenylalanine. In this work, photodissociation dynamics for various phenylalanine chromophores, including, phenylethylamine, N-methyl-phenylethylamine, and N-acetyl phenylalanine methyl ester was investigated in a molecular beam at 248 and 193 nm using multimass ion imaging techniques. The major dissociation channel for these compounds is the C-C bond cleavage. However, the photofragment translational energy distribution of phenylethylamine contains two components. The slow component corresponds to the dissociation on the ground state surface after internal conversion, and the fast component represents the dissociation from an excited state with a large exit barrier. The competition between the dissociation on the ground state and on the excited state changes as the size of chromophores increases. Internal conversion to the ground state prior to dissociation becomes the major nonradiative process for large chromophores. This study reveals the size-dependent photostability for these amino acid chromophores.
Tseng
Chien-Ming
CM
Institute of Atomic and Molecular Sciences, Academia Sinica, P. O. Box: 23-166, Taipei 10617, Taiwan.
Lin
Ming-Fu
MF
Yang
Yi Lin
YL
Ho
Yu Chieh
YC
Ni
Chi-Kung
CK
Chang
Jia-Lin
JL
D010649:Phenylalanine / Q000031:analogs & derivatives*; D055668:Photochemical Processes; D011789:Quantum Theory; D013056:Spectrophotometry, Ultraviolet
D010649:Phenylalanine