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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Fudim, Roman Mehlhorn, Jennifer Berthold, Thomas Weber, Stefan Schleicher, Erik Kennis, John T. M. Mathes, Tilo |
| Description | Country affiliation: Germany Author Affiliation: Fudim R ( Institut für Biologie/Experimentelle Biophysik, Humboldt Universität zu Berlin, Berlin, Germany.); Mehlhorn J ( Institut für Biologie/Experimentelle Biophysik, Humboldt Universität zu Berlin, Berlin, Germany.); Berthold T ( Institut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.); Weber S ( Institut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.); Schleicher E ( Freiburg Institute for Advanced Studies (FRIAS), Albert-Ludwigs-Universität Freiburg, Germany.); Kennis JT ( Institut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.); Mathes T ( Inorganic Chemistry Laboratory, University of Oxford, UK.) |
| Abstract | Blue light receptors using FAD (BLUFs) facilitate blue light-induced signal transduction via light-induced rearrangement of hydrogen bonds between the flavin chromophore and a conserved glutamine side chain. Here, we investigated the photochemistry of the BLUF domain Slr1694 from Synechocystis sp. in which the glutamine side chain was removed. Without the glutamine, no red-shifted signaling state is formed, but light-induced proton-coupled electron transfer between protein and flavin takes place similarly as for the wild-type protein. However, the lifetime of the neutral flavin semiquinone-tyrosyl radical pair is greatly prolonged from < 100 ps to several nanoseconds, which indicates that the formation of radical intermediates drives the hydrogen bond rearrangement in BLUF photoactivation. Moreover, glutamine plays a central role in the molecular organization of the hydrogen bond network in the flavin-binding pocket, as its removal enhances electron transfer from tyrosine to the excited flavin, and enables competing electron transfer from a nearby tryptophan. |
| File Format | HTM / HTML |
| ISSN | 1742464X |
| Issue Number | 16 |
| Volume Number | 282 |
| e-ISSN | 17424658 |
| Journal | FEBS Journal |
| Language | English |
| Publisher | Wiley (on behalf of the Federation of European Biochemical Societies) |
| Publisher Date | 2015-08-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Bacterial Proteins Chemistry Radiation Effects Flavins Photoreceptors, Microbial Synechocystis Amino Acid Substitution Genetics Electron Spin Resonance Spectroscopy Electron Transport Metabolism Free Radicals Glutamine Hydrogen Bonding Light Models, Molecular Mutagenesis, Site-directed Photochemical Processes Protein Structure, Tertiary Recombinant Proteins Signal Transduction Spectrophotometry Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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