R. Diller et al., FEMTOSECOND TIME-RESOLVED INFRARED-LASER STUDY OF THE J-K TRANSITION OF BACTERIORHODOPSIN, Chemical physics letters, 241(1-2), 1995, pp. 109-115
The J-K transition of the bacteriorhodopsin photocycle was monitored b
y sub-picosecond time-resolved infrared spectroscopy. IR difference sp
ectra in the region between 1670 and 1600 cm(-1) were taken at 1.5 and
9 ps, respectively, after photoexcitation of BR(570) at 540 nm. Spect
ral shifts of the bands at 1607 and 1661 cm(-1) reflect the chromophor
ic conformational changes during the J to K transition. Kinetics, take
n at 1640 and 1607 cm(-1), show rise times determined by the dephasing
times of the vibrational modes. The partial decrease of the bleach si
gnal at 1640 cm-l is interpreted as a recovery of the vibrationally co
oled BR(570) electronic ground state and provides a new method to meas
ure the photocycle quantum yield. The development of the bleach at 166
1 cm(-1) occurred faster than 500 fs, suggesting an almost instantaneo
us protein response to the electronic excitation.