(5‐demethyl)‐Bacteriorhodopsin analogue: its formation and light‐driven proton pump action

FEBS Letters

Lugtenburg, J.¹  Rodenburg, L.J.M.¹  Muradin-Szweykowska, M.¹  Dam, K.van²  Amsterdam, L.J.P.van¹  der Bend, R.L.van² 

[1] Department of Organic Chemistry, Leiden University, 2300 RA Leiden, The Netherlands;Department of Chemistry, B.C.P. Jansen Instituut, University of Amsterdam, 1018 TV Amsterdam, The Netherlands

关键词: Halobacterium halobium;    Purple membrane;    Light—dark adaptation;    Light energy conversion;    Proton pump;    Phospholipid vesicle;   

DOI  :  10.1016/0014-5793(83)80899-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The binding of the isomers (all-trans, 13-cis, 11-cis and 9-cis) of 5-demethylretinal to bacterioopsin and the light—dark adaptation as well as the light-driven proton pump action of the resulting bacteriorhodopsin analogue were studied. The (5-demethyl)-bacteriorhodopsinis formed ≈ 3-times faster than unmodified bacteriorhodopsin and shows an efficient light-driven proton pump action. These findings show that upon binding of retinal to bacterioopsin the protein forces the chromophore to adopt a more planar ring-chain conformation than in free retinal.

【 授权许可】

Unknown