Hydrogen atoms are produced when tryptophan within a protein is irradiated with ultraviolet light.
The UV photolysis of the aromatic amino acid, tryptophan (Trp), in the Ca(2+)-binding protein, cod parvalbumin, type III, was studied using electron paramagnetic resonance (EPR) spectroscopy in the temperature range 4-80 K. For the Ca(2+)-bound protein, irradiation with UV light (250-400 nm) resulted in the generation of atomic hydrogen with a hyperfine splitting of 50.9 mT, whereas in the Ca(2+)-free form, where the Trp is exposed to solvent, the trapped atomic hydrogen was not in evidence. In the same spectra, the radical signal in the g = 2.00 region could be detected. The line shape of the Ca(2+)-bound form is similar to the EPR line shape obtained for Trp in micellar systems. In contrast, the EPR line shape for the Ca(2+)-free form is essentially featureless up to 80 K. The EPR spectra of the photoproducts of Trp and the nature of the photoreactions are therefore sensitive to the environment of Trp within the protein.
Angiolillo
P J
PJ
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6089, USA.
Vanderkooi
J M
JM
D000818:Animals; D002118:Calcium / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D005399:Fishes; D006859:Hydrogen / Q000737:chemistry; D010320:Parvalbumins / Q000737:chemistry / Q000528:radiation effects; D010782:Photolysis; D011506:Proteins / Q000737:chemistry / Q000528:radiation effects*; D014364:Tryptophan / Q000737:chemistry / Q000528:radiation effects*; D014466:Ultraviolet Rays
D010320:Parvalbumins; D011506:Proteins; D006859:Hydrogen; D014364:Tryptophan; D002118:Calcium