Sensory rhodopsin I photocycle intermediate SRI380 contains 13‐cis retinal bound via an unprotonated Schiff base
Open Access
- 14 December 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 356 (1) , 25-29
- https://doi.org/10.1016/0014-5793(94)01226-1
Abstract
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.Keywords
This publication has 31 references indexed in Scilit:
- Resonance Raman study of intermediates of the halorhodopsin photocyclePublished by Wiley ,2001
- The Schiff Base Counterion of Bacteriorhodopsin is Protonated in Sensory Rhodopsin I: Spectroscopic and Functional Characterization of the Mutants D76N and D76ABiochemistry, 1994
- A C‐terminal truncation results in high‐level expression of the functional photoreceptor sensory rhodopsin I in the archaeon Halobacterium salinariumMolecular Microbiology, 1993
- Resonance Raman and optical transient studies on the light-induced proton pump of bacteriorhodopsin reveal parallel photocyclesBiochemistry, 1993
- Homologous overexpression of a light‐driven anion pump in an archaebacteriumMolecular Microbiology, 1993
- EVIDENCE THAT THE REPELLENT RECEPTOR FORM OF SENSORY RHODOPSIN I IS AN ATTRACTANT SIGNALING STATE*Photochemistry and Photobiology, 1991
- Solid-state carbon-13 NMR of the retinal chromophore in photointermediates of bacteriorhodopsin: characterization of two forms of MBiochemistry, 1989
- Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212Biochemistry, 1988
- Determination of retinal chromophore structure in bacteriorhodopsin with resonance Raman spectroscopyThe Journal of Membrane Biology, 1985
- Resonance Raman studies of bovine metarhodopsin I and metarhodopsin IIBiochemistry, 1978