作者: Maria MURADIN-SZWEYKOWSKA , Johannes A. PARDOEN , Dick DOBBELSTEIN , AMSTERDAM , Johan LUGTENBURG
DOI: 10.1111/J.1432-1033.1984.TB08082.X
关键词:
摘要: The binding to bacterioopsin of the all-trans isomers retinal analogues lacking six-membered ring and differing in length conjugated chain, as well light-driven action proton pump resulting bacteriorhodopsin analogues, were studied. ‘opsin shifts’ these modified bacteriorhodopsins are all around 2700 cm−1 do not depend on number double bonds chromophore. These experimental results suggest that 4800 cm−1‘opsin shift’ unmodified consists a contribution about due interaction protonated Schiff-base with counterion. extra 2100 shift is specific cyclohexene protein. Only analogue same chromophore itself shows action.