trans-cis Photoisomerization of a photoactive yellow protein model chromophore in crystalline phase.
We have studied the photoinduced trans/cis isomerization of the protonated form of p-hydroxycinnamic thiophenyl ester, a model chromophore of the photoactive yellow protein (PYP), in crystalline phase, by both fluorescence and infrared spectroscopies. The conversion from trans to cis configuration is revealed by a shift of the fluorescence peak and by inspection of the infrared maker bands. The crystal packing apparently stabilizes the cis photoproduct, suggesting different environmental effects from the solvent molecules for this model chromophore in liquid solutions or from the amino acid residues for the PYP chromophore.
Usman
Anwar
A
Masuhara
Hiroshi
H
Asahi
Tsuyoshi
T
D001426:Bacterial Proteins / Q000737:chemistry*; D002627:Chemistry, Physical / Q000379:methods*; D003460:Crystallization; D020607:Halorhodospira halophila / Q000378:metabolism; D008027:Light; D008956:Models, Chemical; D010777:Photochemistry / Q000379:methods*; D020283:Photoreceptors, Microbial / Q000737:chemistry*; D011487:Protein Conformation; D011522:Protons; D012997:Solvents; D013055:Spectrophotometry, Infrared / Q000379:methods
D001426:Bacterial Proteins; D020283:Photoreceptors, Microbial; D011522:Protons; D012997:Solvents; C050162:photoactive yellow protein, Bacteria