Backbone modification of retinal induces protein-like excited state dynamics in solution.
The drastically different reactivity of the retinal chromophore in solution compared to the protein environment is poorly understood. Here, we show that the addition of a methyl group to the C═C backbone of all-trans retinal protonated Schiff base accelerates the electronic decay in solution making...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2012
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| _version_ | 1797097807744598016 |
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| author | Sovdat, T Bassolino, G Liebel, M Schnedermann, C Fletcher, S Kukura, P |
| author_facet | Sovdat, T Bassolino, G Liebel, M Schnedermann, C Fletcher, S Kukura, P |
| author_sort | Sovdat, T |
| collection | OXFORD |
| description | The drastically different reactivity of the retinal chromophore in solution compared to the protein environment is poorly understood. Here, we show that the addition of a methyl group to the C═C backbone of all-trans retinal protonated Schiff base accelerates the electronic decay in solution making it comparable to the proton pump bacteriorhodopsin. Contrary to the notion that reaction speed and efficiency are linked, we observe a concomitant 50% reduction in the isomerization yield. Our results demonstrate that minimal synthetic engineering of potential energy surfaces based on theoretical predictions can induce drastic changes in electronic dynamics toward those observed in an evolution-optimized protein pocket. |
| first_indexed | 2024-03-07T05:00:32Z |
| format | Journal article |
| id | oxford-uuid:d81f9840-e015-4d14-bb63-a933f1cc89a5 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:00:32Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:d81f9840-e015-4d14-bb63-a933f1cc89a52022-03-27T08:46:03ZBackbone modification of retinal induces protein-like excited state dynamics in solution.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d81f9840-e015-4d14-bb63-a933f1cc89a5EnglishSymplectic Elements at Oxford2012Sovdat, TBassolino, GLiebel, MSchnedermann, CFletcher, SKukura, PThe drastically different reactivity of the retinal chromophore in solution compared to the protein environment is poorly understood. Here, we show that the addition of a methyl group to the C═C backbone of all-trans retinal protonated Schiff base accelerates the electronic decay in solution making it comparable to the proton pump bacteriorhodopsin. Contrary to the notion that reaction speed and efficiency are linked, we observe a concomitant 50% reduction in the isomerization yield. Our results demonstrate that minimal synthetic engineering of potential energy surfaces based on theoretical predictions can induce drastic changes in electronic dynamics toward those observed in an evolution-optimized protein pocket. |
| spellingShingle | Sovdat, T Bassolino, G Liebel, M Schnedermann, C Fletcher, S Kukura, P Backbone modification of retinal induces protein-like excited state dynamics in solution. |
| title | Backbone modification of retinal induces protein-like excited state dynamics in solution. |
| title_full | Backbone modification of retinal induces protein-like excited state dynamics in solution. |
| title_fullStr | Backbone modification of retinal induces protein-like excited state dynamics in solution. |
| title_full_unstemmed | Backbone modification of retinal induces protein-like excited state dynamics in solution. |
| title_short | Backbone modification of retinal induces protein-like excited state dynamics in solution. |
| title_sort | backbone modification of retinal induces protein like excited state dynamics in solution |
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