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Absorption and fluorescence spectroscopic characterization of BLUF domain of AppA from Rhodobacter sphaeroides

MPG-Autoren
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Jung,  Astrid
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Heme and Flavin Enzymes, Max Planck Institute for Medical Research, Max Planck Society;
Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Zirak, P., Penzkofer, A., Schiereis, T., Hegemann, P., Jung, A., & Schlichting, I. (2005). Absorption and fluorescence spectroscopic characterization of BLUF domain of AppA from Rhodobacter sphaeroides. Chemical Physics, 315(1), 142-154. doi:10.1016/j.chemphys.2005.04.008.


Zitierlink: http://hdl.handle.net/21.11116/0000-0000-385C-B
Zusammenfassung
The BLUF domain of the transcriptional anti-repressor protein AppA from the non-sulfur anoxyphototrophic purple bacterium Rhodobacter sphaeroides was characterized by absorption and emission spectroscopy. The BLUF domain constructs AppA148 (consisting of amino-acid residues 1–148) and AppA126 (amino-acid residues 1–126) are investigated. The cofactor of the investigated domains is found to consist of a mixture of the flavins riboflavin, FMN, and FAD. The dark-adapted domains exist in two different active receptor conformations (receptor states) with different sub-nanosecond fluorescence lifetimes (BLUFr,f and BLUFr,sl) and a small non-interacting conformation (BLUFnc). The active receptor conformations are transformed to putative signalling states (BLUFs,f and BLUFs,sl) of low fluorescence efficiency and picosecond fluorescence lifetime by blue-light excitation (light-adapted domains). In the dark at room temperature both signalling states recover back to the initial receptor states with a time constant of about 17 min. A quantum yield of signalling state formation of about 25% was determined by intensity dependent transmission measurements. A photo-cycle scheme is presented including photo-induced charge transfer complex formation, charge recombination, and protein binding pocket reorganisation.