Merz, Thomas and Sadeghian, Keyarash and Schuetz, Martin (2011) Why BLUF photoreceptors with roseoflavin cofactors lose their biological functionality. PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 13 (32). pp. 14775-14783. ISSN 1463-9076, 1463-9084
Full text not available from this repository. (Request a copy)Abstract
The photophysics of roseoflavin in three different environments is investigated by using ab initio and quantum mechanics/molecular mechanics methods. Intramolecular charge transfer is shown to be responsible for the quenching of the fluorescence in the gas phase, and in the water environment. However, for the roseoflavin incorporated into the blue light using flavin (BLUF) protein environment (substituting the native flavin) no such deactivation is found. The conical intersection between the locally excited state of the chromophore and the charge transfer state involving the tyrosine residue, which in the native BLUF domain is responsible for initiating the photocycle, is missing for the roseoflavin substituted protein. This explains the experimental observations of the lack of any photocycle, and the loss of the biological function of the BLUF photoreceptor reported earlier.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SYNECHOCYSTIS SP PCC6803; GAUSSIAN-BASIS SETS; INTRAMOLECULAR CHARGE-TRANSFER; MEDIATED SIGNAL-TRANSDUCTION; RHODOBACTER-SPHAEROIDES; LIGHT RECEPTOR; SPECTROSCOPIC CHARACTERIZATION; STRUCTURAL-CHANGES; CRYSTAL-STRUCTURES; PROTEIN SLR1694; |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Research Group Theoretical Chemistry > Prof. Dr. Martin Schütz |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 02 Jul 2020 06:13 |
| Last Modified: | 02 Jul 2020 06:13 |
| URI: | https://pred.uni-regensburg.de/id/eprint/21665 |
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