Sub-picosecond C$=$C bond photo-isomerization: evidence for the role of excited state mixing
Sub-picosecond photo-isomerization is the major primary process of energy conversion in retinal proteins and has as such been in the focus of extensive theoretical and experimental work over the past decades. In this review article, we revisit the long-standing question as to how the protein tunes t...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Académie des sciences
2021-03-01
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| Series: | Comptes Rendus. Physique |
| Subjects: | |
| Online Access: | https://comptes-rendus.academie-sciences.fr/physique/articles/10.5802/crphys.41/ |
| _version_ | 1827785159452131328 |
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| author | Agathangelou, Damianos Roy, Partha Pratim del Carmen Marín, María Ferré, Nicolas Olivucci, Massimo Buckup, Tiago Léonard, Jérémie Haacke, Stefan |
| author_facet | Agathangelou, Damianos Roy, Partha Pratim del Carmen Marín, María Ferré, Nicolas Olivucci, Massimo Buckup, Tiago Léonard, Jérémie Haacke, Stefan |
| author_sort | Agathangelou, Damianos |
| collection | DOAJ |
| description | Sub-picosecond photo-isomerization is the major primary process of energy conversion in retinal proteins and has as such been in the focus of extensive theoretical and experimental work over the past decades. In this review article, we revisit the long-standing question as to how the protein tunes the isomerization speed and quantum yield. We focus on our recent contributions to this field, which underscore the concept of a delicate mixing of reactive and non-reactive excited states, as a result of steric properties and electrostatic interactions with the protein environment. Further avenues and new approaches are outlined which hold promise for advancing our understanding of these intimately coupled chromophore–protein systems. |
| first_indexed | 2024-03-11T16:15:06Z |
| format | Article |
| id | doaj.art-51e43d528caf4e9e86808c541a68c0d2 |
| institution | Directory Open Access Journal |
| issn | 1878-1535 |
| language | English |
| last_indexed | 2024-03-11T16:15:06Z |
| publishDate | 2021-03-01 |
| publisher | Académie des sciences |
| record_format | Article |
| series | Comptes Rendus. Physique |
| spelling | doaj.art-51e43d528caf4e9e86808c541a68c0d22023-10-24T14:21:54ZengAcadémie des sciencesComptes Rendus. Physique1878-15352021-03-0122S211113810.5802/crphys.4110.5802/crphys.41Sub-picosecond C$=$C bond photo-isomerization: evidence for the role of excited state mixingAgathangelou, Damianos0Roy, Partha Pratim1del Carmen Marín, María2Ferré, Nicolas3Olivucci, Massimo4Buckup, Tiago5Léonard, Jérémie6Haacke, Stefan7Université de Strasbourg – CNRS, Institut de Physique et Chimie des Matériaux de Strasbourg, 67034 Strasbourg, FrancePhysikalisch-Chemisches Institut, Ruprecht-Karls Universität Heidelberg, 69120 Heidelberg, GermanyBiotechnology, Pharmacy and Chemistry Department, University of Siena, Siena 53100, ItalyAix-Marseille Univ. – CNRS, ICR, 13397 Marseille, FranceBiotechnology, Pharmacy and Chemistry Department, University of Siena, Siena 53100, Italy; Chemistry Department, Bowling Green State University, Bowling Green, Ohio 43403, USAPhysikalisch-Chemisches Institut, Ruprecht-Karls Universität Heidelberg, 69120 Heidelberg, GermanyUniversité de Strasbourg – CNRS, Institut de Physique et Chimie des Matériaux de Strasbourg, 67034 Strasbourg, FranceUniversité de Strasbourg – CNRS, Institut de Physique et Chimie des Matériaux de Strasbourg, 67034 Strasbourg, FranceSub-picosecond photo-isomerization is the major primary process of energy conversion in retinal proteins and has as such been in the focus of extensive theoretical and experimental work over the past decades. In this review article, we revisit the long-standing question as to how the protein tunes the isomerization speed and quantum yield. We focus on our recent contributions to this field, which underscore the concept of a delicate mixing of reactive and non-reactive excited states, as a result of steric properties and electrostatic interactions with the protein environment. Further avenues and new approaches are outlined which hold promise for advancing our understanding of these intimately coupled chromophore–protein systems.https://comptes-rendus.academie-sciences.fr/physique/articles/10.5802/crphys.41/Photo-isomerisationRetinal proteinsChromophore–protein couplingNon-adiabatic dynamicsPhoto-sensory proteinsCharge transfer state |
| spellingShingle | Agathangelou, Damianos Roy, Partha Pratim del Carmen Marín, María Ferré, Nicolas Olivucci, Massimo Buckup, Tiago Léonard, Jérémie Haacke, Stefan Sub-picosecond C$=$C bond photo-isomerization: evidence for the role of excited state mixing Comptes Rendus. Physique Photo-isomerisation Retinal proteins Chromophore–protein coupling Non-adiabatic dynamics Photo-sensory proteins Charge transfer state |
| title | Sub-picosecond C$=$C bond photo-isomerization: evidence for the role of excited state mixing |
| title_full | Sub-picosecond C$=$C bond photo-isomerization: evidence for the role of excited state mixing |
| title_fullStr | Sub-picosecond C$=$C bond photo-isomerization: evidence for the role of excited state mixing |
| title_full_unstemmed | Sub-picosecond C$=$C bond photo-isomerization: evidence for the role of excited state mixing |
| title_short | Sub-picosecond C$=$C bond photo-isomerization: evidence for the role of excited state mixing |
| title_sort | sub picosecond c c bond photo isomerization evidence for the role of excited state mixing |
| topic | Photo-isomerisation Retinal proteins Chromophore–protein coupling Non-adiabatic dynamics Photo-sensory proteins Charge transfer state |
| url | https://comptes-rendus.academie-sciences.fr/physique/articles/10.5802/crphys.41/ |
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