CHANGES IN STRUCTURE OF THE CHROMOPHORE IN THE PHOTOCHEMICAL PROCESS OF BOVINE RHODOPSIN AS REVEALED BY FTIR SPECTROSCOPY FOR HYDROGEN OUT-OF-PLANE VIBRATIONS
Yj. Ohkita et al., CHANGES IN STRUCTURE OF THE CHROMOPHORE IN THE PHOTOCHEMICAL PROCESS OF BOVINE RHODOPSIN AS REVEALED BY FTIR SPECTROSCOPY FOR HYDROGEN OUT-OF-PLANE VIBRATIONS, Biophysical chemistry, 56(1-2), 1995, pp. 71-78
The hydrogen out-of-plane bending (HOOP) vibrations were studied in th
e difference Fourier transform infrared spectra of lumirhodopsin and m
etarhodopsin I by use of a series of specifically deuterated retinal d
erivatives of bovine rod outer segments. The 947 cm(-1) band of lumirh
odopsin and the 950 cm(-1) band of metarhodopsin I were assigned to th
e mode composed of both 11-HOOP and 12-HOOP vibrations. This result su
ggests that the perturbation near C-12-H of the retinal in the earlier
intermediate, bathorhodopsin (Palings, van den Berg, Lugtenburg and M
athies, Biochemistry, 28 (1989) 1498-1507), is extinguished in lumirho
dopsin 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 i
n the 12-D derivatives. The result suggests a change in geometrical al
ignment of the C-14-H bond in lumirhodopsin with respect to the N-H bo
nd of the Schiff base.