STRUCTURE OF HYPSORHODOPSIN: ANALYSIS BY FOURIER TRANSFORM INFRARED SPECTROSCOPY AT 10 K
作者： Jun Sasaki , Akio Maeda , Yoshinori Shichida , Michel Groesbeek , Johan Lugtenburg
DOI: 10.1111/J.1751-1097.1992.TB09730.X
关键词:
摘要: — Vibrational bands of hypsorhodopsin in the difference Fourier transform infrared spectra were identified as which arose after formation isorhodopsin by successive irradiations bovine rhodopsin at 10 K with >500 nm light, and also disappeared upon conversion to bathorhodopsin warming. The chromophore assigned shifted deuterium substitution polyene chain retinylidene chromophore. presence shift D2O exchange clearly shows that Schiff base is protonated. amide I several other protein appeared same frequencies those bathorhodopsin, but they are different from isorhodopsin. Furthermore, like displays Cl—H out-of-plane bending mode weakly coupled C12--–H mode. These facts show has a conformation chromophore-opsin interaction more similar than
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