Absorption Studies of Neutral Retinal Schiff Base Chromophores
| Autor: | Mogens Brøndsted Nielsen, I. B. Nielsen, Lars H. Andersen, Lutz Lammich, Michael Åxman Petersen |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Rhodopsin
Time Factors Light Absorption spectroscopy Ultraviolet Rays Static Electricity Enzyme-Linked Immunosorbent Assay Protonation Photochemistry Retina chemistry.chemical_compound Deprotonation Animals Humans Physical and Theoretical Chemistry Schiff Bases Schiff base biology Retinal Chromophore Models Chemical chemistry Spectrophotometry Solvents biology.protein Protons Absorption (chemistry) Signal Transduction |
| Zdroj: | Nielsen, I B, Petersen, M Å, Lammich, L, Brøndsted Nielsen, M & Andersen, L H 2006, ' Absorption Studies of Neutral Retinal Schiff Base Chromophores ', Journal of Physical Chemistry Part A: Molecules, Spectroscopy, Kinetics, Environment and General Theory, vol. 110, pp. 12592-12596 . |
| ISSN: | 1520-5215 1089-5639 |
| DOI: | 10.1021/jp064901r |
| Popis: | The neutral retinal Schiff base is connected to opsin in UV sensing pigments and in the blue-shifted meta-II signaling state of the rhodopsin photocycle. We have designed and synthesized two model systems for this neutral chromophore and have measured their gas-phase absorption spectra in the electrostatic storage ring ELISA with a photofragmentation technique. By comparison to the absorption spectrum of the protonated retinal Schiff base in vacuo, we found that the blue shift caused by deprotonation of the Schiff base is more than 200 nm. The absorption properties of the UV absorbing proteins are thus largely determined by the intrinsic properties of the chromophore. The effect of approaching a positive charge to the Schiff base was also studied, as well as the susceptibility of the protonated and unprotonated chromophores to experience spectral shifts in different solvents. |
| Databáze: | OpenAIRE |
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