Bathorhodopsin intermediates from 11-cis-rhodopsin and 9-cis-rhodopsin.
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منابع مشابه
Bathorhodopsin intermediates from 11-cis-rhodopsin and 9-cis-rhodopsin.
Bathorhodopsin-rhodopsin difference spectra of native 11-cis-rhodopsin and regenerated 9-cis-rhodopsin were measured at room temperature with a double-beam laser spectrophotometer after excitation at 532 nm. A detailed analysis of data obtained at 85 psec after excitation suggests that the bathorhodopsins generated from 11-cis- and 9-cis-rhodopsin differ in their extinction coefficients and tha...
متن کاملPartial agonist activity of 11-cis-retinal in rhodopsin mutants.
Rhodopsin, the photoreceptor molecule of the vertebrate rod cell, is a G protein-coupled receptor. Rhodopsin consists of the opsin apoprotein and its 11-cis-retinal chromophore, which is covalently bound to a specific lysine residue by a stable protonated Schiff base linkage. Rhodopsin activation occurs when light causes photoisomerization of the 11-cis chromophore to its all-trans form. The al...
متن کاملOrigin of Fluorescence in 11-cis Locked Bovine Rhodopsin.
The excited state lifetime of bovine rhodopsin (Rh) increases from ca. 100 fs to 85 ps when the C11═C12 bond of its chromophore is locked by a cyclopentene moiety (Rh5). To explain such an increase, we employed ab initio multiconfigurational quantum chemistry to construct computer models of Rh and Rh5 and to investigate the shape of their excited state potential energy surfaces in a comparative...
متن کاملMeasurement of Slow Spontaneous Release of 11-cis-Retinal from Rhodopsin.
The vertebrate visual photoreceptor rhodopsin (Rho) is a unique G protein-coupled receptor as it utilizes a covalently tethered inverse agonist (11-cis-retinal) as the native ligand. Previously, electrophysiological studies showed that ligand binding of 11-cis-retinal in dark-adapted Rho was essentially irreversible with a half-life estimated to be 420 years, until after thermal isomerization t...
متن کاملBiochemical and physiological properties of rhodopsin regenerated with 11-cis-6-ring- and 7-ring-retinals.
Phototransduction is initiated by the photoisomerization of rhodopsin (Rho) chromophore 11-cis-retinylidene to all-trans-retinylidene. Here, using Rho regenerated with retinal analogs with different ring sizes, which prevent isomerization around the C(11)=C(12) double bond, the activation mechanism of this G-protein-coupled receptor was investigated. We demonstrate that 11-cis-7-ring-Rho does n...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1983
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.80.7.1887