|
ИСТИНА |
Войти в систему Регистрация |
Интеллектуальная Система Тематического Исследования НАукометрических данных |
||
Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsinстатья
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или Scopus- Авторы: Kovacs Gabriela Nass, Colletier Jacques-Philippe, Grünbein Marie Luise, Yang Yang, Stensitzki Till, Batyuk Alexander, Carbajo Sergio, Bruce Doak R., Ehrenberg David, Foucar Lutz, Gasper Raphael, Gorel Alexander, Hilpert Mario, Kloos Marco, Koglin Jason E., Reinstein Jochen, Roome Christopher M., Schlesinger Ramona, Seaberg Matthew, Shoeman Robert L., Stricker Miriam, Boutet Sébastien, Haacke Stefan, Heberle Joachim, Heyne Karsten, Domratcheva Tatiana, Barends Thomas R.M., Schlichting Ilme
- Журнал: Nature communications
- Том: 10
- Номер: 1
- Год издания: 2019
- Издательство: Nature Pub. Group
- Местоположение издательства: United Kingdom
- DOI: 10.1038/s41467-019-10758-0
- Аннотация: Bacteriorhodopsin (bR) is a light-driven proton pump. The primary photochemical event upon light absorption is isomerization of the retinal chromophore. Here we used time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy were used to identify a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multiphoton effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins.
- Добавил в систему: Домрачева Татьяна Михайловна