Raman Vibrational Signatures of Excited States of Echinenone in the Orange Carotenoid Protein (OCP) and Implications for its Photoactivation Mechanism
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F24%3A43908439" target="_blank" >RIV/60076658:12310/24:43908439 - isvavai.cz</a>
Alternative codes found
RIV/CZ______:_____/24:N0000042
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0022283624002201?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0022283624002201?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jmb.2024.168625" target="_blank" >10.1016/j.jmb.2024.168625</a>
Alternative languages
Result language
angličtina
Original language name
Raman Vibrational Signatures of Excited States of Echinenone in the Orange Carotenoid Protein (OCP) and Implications for its Photoactivation Mechanism
Original language description
In this study, the vibrational characteristics of optically excited echinenone in various solvents and the Orange Carotenoid Protein (OCP) in red and orange states are systematically investigated through steady-state and time-resolved spectroscopy techniques. Time-resolved experiments, employing both Transient Absorption (TA) and Femtosecond Stimulated Raman Spectroscopy (FSRS), reveal different states in the OCP photoactivation process. The time-resolved studies indicate vibrational signatures of exited states positioned above the S1 1 state during the initial 140 fs of carotenoid evolution in OCP, an absence of a vibrational signature for the relaxed S1 1 state of echinenone in OCP, and more robust signatures of a highly excited ground state (GS) in OCP. Differences in S1 1 state vibration population signatures between OCP and solvents are attributed to distinct conformations of echinenone in OCP and hydrogen bonds at the keto group forming a short-lived intramolecular charge transfer (ICT) state. The vibrational dynamics of the hot GS in OCP show a more pronounced red shift of ground state C@C vibration compared to echinenone in solvents, thus suggesting an unusually hot form of GS. The study proposes a hypothesis for the photoactivation mechanism of OCP, emphasizing the high level of vibrational excitation in longitudinal stretching modes as a driving force. In conclusion, the comparison of vibrational signatures reveals unique dynamics of energy dissipation in OCP, providing insights into the photoactivation mechanism and highlighting the impact of the protein environment on carotenoid behavior. The study underscores the importance of vibrational analysis in understanding the intricate processes involved in early phase OCP photoactivation. (c) 2024 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Molecular Biology
ISSN
0022-2836
e-ISSN
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Volume of the periodical
436
Issue of the periodical within the volume
16
Country of publishing house
GB - UNITED KINGDOM
Number of pages
17
Pages from-to
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UT code for WoS article
001285767800001
EID of the result in the Scopus database
2-s2.0-85195031167