Picosecond protein response to the chromophore isomerization of photoactive yellow protein: selective observation of tyrosine and tryptophan residues by time-resolved ultraviolet resonance Raman spectroscopy.
Picosecond time-resolved ultraviolet resonance Raman (UVRR) spectra of photoactive yellow protein (PYP) were measured. UVRR bands attributed to the vibration of tyrosine and tryptophan residues showed a spectral change upon photoreaction. It was found that the hydrogen-bond strength between the chromophore and Y42 increases in the pG* state. The ultrafast change in the tryptophan band revealed that a photoinduced structural change of the chromophore had propagated to the W119 region, located 12 A from the chromophore, within picoseconds.
Mizuno
Misao
M
Hamada
Norio
N
Tokunaga
Fumio
F
Mizutani
Yasuhisa
Y
D001426:Bacterial Proteins / Q000737:chemistry*; D020283:Photoreceptors, Microbial / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman; D013997:Time Factors; D014364:Tryptophan / Q000737:chemistry*; D014443:Tyrosine / Q000737:chemistry*
D001426:Bacterial Proteins; D020283:Photoreceptors, Microbial; C050162:photoactive yellow protein, Bacteria; D014443:Tyrosine; D014364:Tryptophan