Structural Information about the ...
Document type :
Article dans une revue scientifique: Article original
PMID :
Permalink :
Title :
Structural Information about the <i>trans</i>-to- <i>cis</i> Isomerization Mechanism of the Photoswitchable Fluorescent Protein rsEGFP2 Revealed by Multiscale Infrared Transient Absorption.
Author(s) :
Uriarte, Lucas M. [Auteur]
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement - UMR 8516 [LASIRE]
Vitale, Raffaele [Auteur]
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement (LASIRE) - UMR 8516
Niziński, Stanislaw [Auteur]
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement - UMR 8516 [LASIRE]
Uniwersytet im. Adama Mickiewicza w Poznaniu = Adam Mickiewicz University in Poznań [UAM]
Hadjidemetriou, Kyprianos [Auteur]
Institut de biologie structurale [IBS - UMR 5075]
Zala, N. [Auteur]
Institut de biologie structurale [IBS - UMR 5075]
Lukacs, A. [Auteur]
Greetham, G. M. [Auteur]
Sazanovich, I. V. [Auteur]
Weik, M. [Auteur]
Institut de biologie structurale [IBS - UMR 5075]
Ruckebusch, Cyril [Auteur]
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement (LASIRE) - UMR 8516
Meech, S. R. [Auteur]
Sliwa, Michel [Auteur]
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement (LASIRE) - UMR 8516
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement - UMR 8516 [LASIRE]
Vitale, Raffaele [Auteur]
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement (LASIRE) - UMR 8516
Niziński, Stanislaw [Auteur]
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement - UMR 8516 [LASIRE]
Uniwersytet im. Adama Mickiewicza w Poznaniu = Adam Mickiewicz University in Poznań [UAM]
Hadjidemetriou, Kyprianos [Auteur]
Institut de biologie structurale [IBS - UMR 5075]
Zala, N. [Auteur]
Institut de biologie structurale [IBS - UMR 5075]
Lukacs, A. [Auteur]
Greetham, G. M. [Auteur]
Sazanovich, I. V. [Auteur]
Weik, M. [Auteur]
Institut de biologie structurale [IBS - UMR 5075]
Ruckebusch, Cyril [Auteur]
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement (LASIRE) - UMR 8516
Meech, S. R. [Auteur]
Sliwa, Michel [Auteur]
Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement (LASIRE) - UMR 8516
Journal title :
Journal of Physical Chemistry Letters
Abbreviated title :
J Phys Chem Lett
Pages :
1194-1202
Publication date :
2022-01-29
ISSN :
1948-7185
English keyword(s) :
4 Vibrational time-resolved (TR)
1
crystallography (TR-SFX)]
1
crystallography (TR-SFX)]
HAL domain(s) :
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]
English abstract : [en]
RsEGFP2 is a reversibly photoswitchable fluorescent protein used in super-resolved optical microscopies, which can be toggled between a fluorescent On state and a nonfluorescent Off state. Previous time-resolved ...
Show more >RsEGFP2 is a reversibly photoswitchable fluorescent protein used in super-resolved optical microscopies, which can be toggled between a fluorescent On state and a nonfluorescent Off state. Previous time-resolved ultraviolet–visible spectroscopic studies have shown that the Off-to-On photoactivation extends over the femto- to millisecond time scale and involves two picosecond lifetime excited states and four ground state intermediates, reflecting a trans-to-cis excited state isomerization, a millisecond deprotonation, and protein structural reorganizations. Femto- to millisecond time-resolved multiple-probe infrared spectroscopy (TRMPS-IR) can reveal structural aspects of intermediate species. Here we apply TRMPS-IR to rsEGFP2 and implement a Savitzky–Golay derivative analysis to correct for baseline drift. The results reveal that a subpicosecond twisted excited state precursor controls the trans-to-cis isomerization and the chromophore reaches its final position in the protein pocket within 100 ps. A new step with a time constant of 42 ns is reported and assigned to structural relaxation of the protein that occurs prior to the deprotonation of the chromophore on the millisecond time scale.Show less >
Show more >RsEGFP2 is a reversibly photoswitchable fluorescent protein used in super-resolved optical microscopies, which can be toggled between a fluorescent On state and a nonfluorescent Off state. Previous time-resolved ultraviolet–visible spectroscopic studies have shown that the Off-to-On photoactivation extends over the femto- to millisecond time scale and involves two picosecond lifetime excited states and four ground state intermediates, reflecting a trans-to-cis excited state isomerization, a millisecond deprotonation, and protein structural reorganizations. Femto- to millisecond time-resolved multiple-probe infrared spectroscopy (TRMPS-IR) can reveal structural aspects of intermediate species. Here we apply TRMPS-IR to rsEGFP2 and implement a Savitzky–Golay derivative analysis to correct for baseline drift. The results reveal that a subpicosecond twisted excited state precursor controls the trans-to-cis isomerization and the chromophore reaches its final position in the protein pocket within 100 ps. A new step with a time constant of 42 ns is reported and assigned to structural relaxation of the protein that occurs prior to the deprotonation of the chromophore on the millisecond time scale.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Collections :
Submission date :
2024-02-28T22:33:28Z
2024-03-20T09:01:54Z
2024-03-20T09:01:54Z