Spectroscopy and photoisomerization of protonated Schiff-base retinal derivatives in vacuo
| Autor: | Ricky Teiwes, Mordechai Sheves, Anne Pilgaard Rasmussen, Elisabeth Gruber, Lars H. Andersen |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
DYNAMICS
ISOMERIZATION Schiff base biology Photoisomerization BACTERIORHODOPSIN ALL-TRANS PROTEIN CHROMOPHORES General Physics and Astronomy Retinal Bacteriorhodopsin Protonation ELECTROSTATIC STORAGE-RING Chromophore RHODOPSIN Photochemistry ABSORPTION-SPECTRA chemistry.chemical_compound chemistry Rhodopsin biology.protein Physical and Theoretical Chemistry FLUORESCENCE Isomerization |
| Zdroj: | Rasmussen, A P, Gruber, E, Teiwes, R, Sheves, M & Andersen, L H 2021, ' Spectroscopy and photoisomerization of protonated Schiff-base retinal derivatives in vacuo ', Physical Chemistry Chemical Physics, vol. 23, no. 48, pp. 27227-27233 . https://doi.org/10.1039/d1cp04501f |
| Popis: | The protonated Schiff-base retinal acts as the chromophore in bacteriorhodopsin as well as in rhodopsin. In both cases, photoexcitation initializes fast isomerization which eventually results in storage of chemical energy or signaling. The details of the photophysics for this important chromophore is still not fully understood. In this study, action-absorption spectra and photoisomerization dynamics of three retinal derivatives are measured in the gas phase and compared to that of the protonated Schiff-base retinal. The retinal derivatives include C-9=C-10 trans-locked, C-13=C-14 trans-locked and a retinal derivative without the beta-ionone ring. The spectroscopy as well as the isomerization speed of the chromophores are altered significantly as a consequence of the steric constraints. |
| Databáze: | OpenAIRE |
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