Existence of two L photointermediates of halorhodopsin from Halobacterium salinarium, differing in their protein and water FTIR bands.
FTIR difference spectra were recorded for the photoreactions of halorhodopsin from Halobacterium salinarium at 170 and 250 K. Obvious differences at the two temperatures were noted in neither the visible spectra nor the FTIR bands of the chromophore. However, perturbation of Asp141 is observed in the L intermediate at 250 K but not at 170 K. We named these photoproducts La (at 170 K) and Lb (at 250 K). The spectrum of Lb is distinct from that of La also in the different shifts of water O-H stretching bands, and larger changes in the bands from the protein backbone with different sensitivities to varying the halide. These results suggest that the photocycle of halorhodopsin contains two L states, La and Lb, in which the structure of protein and internal water molecules is different but chloride stays at the same site close to the Schiff base.
Department of Biophysics, Graduate School of Science, Kyoto University, Japan.
Y S
YS
Chon
H
H
Kandori
J
J
Sasaki
J K
JK
Lanyi
R
R
Needleman
A
A
Maeda
D001436:Bacteriorhodopsins / Q000737:chemistry* / Q000378:metabolism; D001965:Bromides / Q000737:chemistry; D002712:Chlorides / Q000737:chemistry; D003080:Cold Temperature; D019617:Halobacterium salinarum / Q000737:chemistry* / Q000378:metabolism; D025602:Halorhodopsins; D007454:Iodides / Q000737:chemistry; D008027:Light; D010777:Photochemistry; D011487:Protein Conformation; D012172:Retinaldehyde / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared; D014867:Water / Q000737:chemistry* / Q000378:metabolism
D001965:Bromides; D002712:Chlorides; D025602:Halorhodopsins; D007454:Iodides; D014867:Water; D001436:Bacteriorhodopsins; D012172:Retinaldehyde