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Single Hydrogen Bond Donation from Flavin N5 to Proximal Asparagine Ensures FAD Reduction in DNA Photolyaseстатья
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: 11 ноября 2019 г.
- Авторы: Mahaputra Wijaya I.M, Domratcheva Tatiana, Iwata Tatsuya, Getzoff Elizabeth D., Kandori Hideki
- Журнал: Journal of the American Chemical Society
- Том: 138
- Номер: 13
- Год издания: 2016
- Издательство: American Chemical Society
- Местоположение издательства: United States
- Первая страница: 4368
- Последняя страница: 4376
- DOI: 10.1021/jacs.5b10533
- Аннотация: The spread of the absorbance of the stable FADH• radical (300–700 nm) allows CPD photolyase to highly efficiently form FADH–, making it functional for DNA repair. In this study, FTIR spectroscopy detected a strong hydrogen bond, from FAD N5–H to the carbonyl group of the Asn378 side chain, that is modulated by the redox state of FAD. The observed characteristic frequency shifts were reproduced in quantum-mechanical models of the flavin binding site, which were then employed to elucidate redox tuning governed by Asn378. We demonstrate that enhanced hydrogen bonding of the Asn378 side chain with the FADH• radical increases thermodynamic stabilization of the radical state, and further ensures kinetic stabilization and accumulation of the fully reduced FADH– state.
- Добавил в систему: Домрачева Татьяна Михайловна