Electrochromic shift calculations exhibit the light-activation mechanism of BLUF photoreceptors
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78. Jahrestagung der DPG und DPG-Frühjahrstagung
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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-bonding pattern surrounding the chromophore . Two opposite molecular models exist. One model is supported by the majority of crystallographic studies , whereas the second is favored by most spectroscopical works . 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. Our calculations accurately reproduce a series of spectroscopic data and provide compelling evidence for the model supported by the majority of crystallographic studies .
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