Electrochromic shift calculations exhibit the light-activation mechanism of BLUF photoreceptors
Sprache des Vortragstitels:
Englisch
Original Tagungtitel:
Current Challenges in Supramolecular Artificial Photosynthesis
Sprache des Tagungstitel:
Englisch
Original Kurzfassung:
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 [1]. Two opposite structural models exist, named in the literature ?tryptophan-in? [2] and ?tryptophan-out? [3]. 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 [4].
[1] Masuda, S., Plant Cell Physiol. 54, 171 (2013).
[2] Anderson, S. et al., Biochemistry 44, 7998 (2005).
[3] Jung, A. et al., Proc. Natl. Acad. Sci. U.S.A. 102, 12350 (2005).
[4] Collette, F. et al., J. Phys. Chem. B 118, 11109 (2014).
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