Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence
Femtosecond-resolved fluorescence of bacterial thymidilate synthase using a Kerr-gate based setup identifies a close-by tyrosine involved in flavin fluorescence quenching, shows that the substrate dUMP acts as a strong quencher itself and highlights functional configurational flexibility
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
EDP Sciences
2013-03-01
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| Series: | EPJ Web of Conferences |
| Online Access: | http://dx.doi.org/10.1051/epjconf/20134107011 |
| _version_ | 1818900435609583616 |
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| author | Liebl U. Myllykallio H. Bouzhir-Sima L. Laptenok S. P. Vos M. H. |
| author_facet | Liebl U. Myllykallio H. Bouzhir-Sima L. Laptenok S. P. Vos M. H. |
| author_sort | Liebl U. |
| collection | DOAJ |
| description | Femtosecond-resolved fluorescence of bacterial thymidilate synthase using a Kerr-gate based setup identifies a close-by tyrosine involved in flavin fluorescence quenching, shows that the substrate dUMP acts as a strong quencher itself and highlights functional configurational flexibility |
| first_indexed | 2024-12-19T20:03:49Z |
| format | Article |
| id | doaj.art-44dd7ce8cf034cdd9454bc12a321701e |
| institution | Directory Open Access Journal |
| issn | 2100-014X |
| language | English |
| last_indexed | 2024-12-19T20:03:49Z |
| publishDate | 2013-03-01 |
| publisher | EDP Sciences |
| record_format | Article |
| series | EPJ Web of Conferences |
| spelling | doaj.art-44dd7ce8cf034cdd9454bc12a321701e2022-12-21T20:07:34ZengEDP SciencesEPJ Web of Conferences2100-014X2013-03-01410701110.1051/epjconf/20134107011Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescenceLiebl U.Myllykallio H.Bouzhir-Sima L.Laptenok S. P.Vos M. H.Femtosecond-resolved fluorescence of bacterial thymidilate synthase using a Kerr-gate based setup identifies a close-by tyrosine involved in flavin fluorescence quenching, shows that the substrate dUMP acts as a strong quencher itself and highlights functional configurational flexibilityhttp://dx.doi.org/10.1051/epjconf/20134107011 |
| spellingShingle | Liebl U. Myllykallio H. Bouzhir-Sima L. Laptenok S. P. Vos M. H. Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence EPJ Web of Conferences |
| title | Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence |
| title_full | Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence |
| title_fullStr | Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence |
| title_full_unstemmed | Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence |
| title_short | Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence |
| title_sort | configurational fluctuations and flavin substrate interactions in the flavoenzyme thyx studied by time and spectrally resolved fluorescence |
| url | http://dx.doi.org/10.1051/epjconf/20134107011 |
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