Sensory rhodopsin I photocycle intermediate SRI380 contains 13‐cis retinal bound via an unprotonated Schiff base

FEBS Letters

Eisfeld, Wolf¹  Haupts, Ulrich²  Stockburger, Manfred¹  Oesterhelt, Dieter² 

[1] Max-Planck Institut für Biophysikalische Chemie, Am Fassberg, D-37077 Göttingen, Germany;Max-Planck Institut für Biochemie, Am Klopferspitz 18a, D-82152 Martinsried, Germany

关键词: Sensory rhodopsin;    Resonance Raman;    Isomerization;   

DOI  :  10.1016/0014-5793(94)01226-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sensory rhodopsin I (SRI), the mutated derivative SRI-D76N and the complex of SRI with its transducer HtrI were overexpressed in Halobacterium salinarium and analyzed by resonance Raman spectroscopy. In the initial state SRI contains all-trans retinal bound via a protonated Schiff base as confirmed by retinal extraction which yields 95 ± 3% all-trans retinal. The photocycle intermediate absorbing maximally at 380 nm (SRI₃₈₀) contains a Schiff base linkage between the protein and 13-cis retinal. Extraction of illuminated SRI yields up to 93% 13-cis retinal. Neither the mutation D76N nor HtrI changed the vibrational pattern of the chromophore.

【 授权许可】

Unknown