Changes in structure of the chromophore in the photochemical process of bovine rhodopsin as revealed by FTIR spectroscopy for hydrogen out-of-plane vibrations.
The hydrogen out-of-plane bending (HOOP) vibrations were studied in the difference Fourier transform infrared spectra of lumirhodopsin and metarhodopsin I by use of a series of specifically deuterated retinal derivatives of bovine rod outer segments. The 947 cm-1 band of lumirhodopsin and the 950 cm-1 band of metarhodopsin I were assigned to the mode composed of both 11-HOOP and 12-HOOP vibrations. This result suggests that the perturbation near C12-H of the retinal in the earlier intermediate, bathorhodopsin (Palings, van den Berg, Lugtenburg and Mathies, Biochemistry, 28 (1989) 1498-1507), is extinguished in lumirhodopsin and metarhodopsin I. Unphotolyzed rhodopsin and metarhodopsin I exhibited the 14-HOOP bands in the 12-D derivatives at 901 and 886 cm-1, respectively. Lumirhodopsin, however, did not show the 14-HOOP in the 12-D derivatives. The result suggests a change in geometrical alignment of the C14-H bond in lumirhodopsin with respect to the N-H bond of the Schiff base.
Ohkita
Y J
YJ
Department of Biophysics, Faculty of Science, Kyoto University, Japan.
Sasaki
J
J
Maeda
A
A
Yoshizawa
T
T
Groesbeek
M
M
Verdegem
P
P
Lugtenburg
J
J
D000818:Animals; D002417:Cattle; D003903:Deuterium; D006859:Hydrogen; D010777:Photochemistry; D011487:Protein Conformation; D012243:Rhodopsin / Q000031:analogs & derivatives / Q000737:chemistry* / Q000378:metabolism*; D017299:Rod Opsins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods; D014732:Vibration
D017299:Rod Opsins; C018586:lumirhodopsin; C013110:metarhodopsins; D006859:Hydrogen; D012243:Rhodopsin; D003903:Deuterium