WATER STRUCTURAL-CHANGES IN THE BACTERIORHODOPSIN PHOTOCYCLE - ANALYSIS BY FOURIER-TRANSFORM INFRARED-SPECTROSCOPY

被引:116
作者
MAEDA, A [1 ]
SASAKI, J [1 ]
SHICHIDA, Y [1 ]
YOSHIZAWA, T [1 ]
机构
[1] UNIV ELECTROCOMMUN, CHOFU, TOKYO 182, JAPAN
关键词
D O I
10.1021/bi00117a023
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Fourier transform infrared difference spectra between light-adapted bacteriorhodopsin (BR) and its photointermediates, L and M, were analyzed for the 3750-3450-cm-1 region. The 0-H stretching vibrational bands were identified from spectra upon substitution with (H2O)-H-2. Among them, the 3642-cm-1 band of BR was assigned to water by substitution with (H2O)-O-18. By a comparison with the published infrared spectra of the water in model systems [Mohr, S. C., Wilk, W. D., & Barrow, G. M. (1965) J. Am. Chem. Soc. 87, 3048-3052], it is shown that the O-H bonds of the water in BR interact very weakly. Upon formation of L, the interaction becomes stronger. The O-H bonds of the protein side chain undergo similar changes. On the other hand, M formation further weakens the interaction of the same water molecules in BR. The appearance of a sharp band at 3486 cm-1, which was assigned tentatively to the N-H stretching vibration of the peptide bond, is unique to L. The results suggest that the water molecules are involved in the perturbation of Asp-96 in the L intermediate and that they are exerted from the protonated Schiff base which changes position upon the light-induced reaction.
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页码:462 / 467
页数:6
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