Electrochromic shift calculations exhibit the light-activation mechanism of BLUF photoreceptors
Sprache des Vortragstitels:
Current Challenges in Supramolecular Artificial Photosynthesis
Sprache des Tagungstitel:
The photoreceptor family named BLUF, short for ?sensors of blue-light using flavin adenine dinucleotide (FAD)?, is involved in a variety of important physiological reactions like phototaxis, photosynthetic gene regulation and virulence. Upon illumination with blue light, the photoreceptor switches into a light-adapted signaling state, with a measurable 10 to 15 nm redshift of the absorption maximum. The spectroscopic shift is explained by an alteration in the hydrogen bond pattern surrounding the chromophore . Two opposite structural models exist, named in the literature ?tryptophan-in?  and ?tryptophan-out? . Within the framework of a quantum chemical/electrostatic calculation scheme, we estimated absorption shifts of the flavin chromophore for a series of site-directed mutants and different BLUF proteins .
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