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How far can a single hydrogen bond tune the spectral properties of the GFP chromophore?статья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 19 сентября 2015 г.
- Авторы: Kiefer Hjalte V., Lattouf Elie, Persen Natascha W., Bochenkova Anastasia V., Andersen Lars H.
- Журнал: Physical Chemistry Chemical Physics
- Том: 17
- Номер: 31
- Год издания: 2015
- Издательство: Royal Society of Chemistry
- Местоположение издательства: United Kingdom
- Первая страница: 20056
- Последняя страница: 20060
- DOI: 10.1039/C5CP02764K
- Аннотация: Photoabsorption of the hydrogen-bonded complex of a neutral and an anionic Green Fluorescent Protein chromophore has been studied using a new dual-detection approach to action-absorption spectroscopy. Following absorption of one photon, dissociation through a single channel ensures that the full absorption spectrum is measured. Our theoretical account of the spectral shape reveals that the anionic 0-0 transition (464 nm) is blue-shifted compared to that of the wild-type protein (478 nm) due to the stronger H-bond in the dimer, and represents an upper bound for that of the isolated anion. At the same time, the apparent effect of the H-bond for the neutral chromophore is as large as 0.5 eV, red-shifting the absorption maximum of the isolated neutral (340 nm) to that measured in the dimer (393 nm) and various proteins ([similar]395 nm). This shift results from changes in the topography of potential-energy surfaces in the Franck-Condon region of the H-bonded systems.
- Добавил в систему: Боченкова Анастасия Владимировна