Structural changes in bacteriorhodopsin during the photocycle measured by time-resolved polarized Fourier transform infrared spectroscopy.
The structural changes in bacteriorhodopsin during the photocycle are investigated. Time resolved polarized infrared spectroscopy in combination with photoselection is used to determine the orientation and motion of certain structural units of the molecule: Asp-85, Asp-96, Asp-115, the Schiff base, and several amide I vibrations. The results are compared with recently published x-ray diffraction data with atomic resolution about conformational motions during the photocycle. The orientation of the measured vibrations are also calculated from the structure data, and based on the comparison of the values from the two techniques new information is obtained: several amide I bands in the infrared spectrum are assigned, and we can also identify the position of the proton in the protonated Asp residues.
Kelemen
L
L
Institute of Biophysics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged H-6701, Hungary.
Ormos
P
P
D001224:Aspartic Acid / Q000737:chemistry; D001436:Bacteriorhodopsins / Q000737:chemistry*; D006217:Halobacterium / Q000378:metabolism; D008027:Light; D016011:Normal Distribution; D010777:Photochemistry; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*; D013997:Time Factors; D014961:X-Ray Diffraction
D001224:Aspartic Acid; D001436:Bacteriorhodopsins