Light-induced dynamics changes of a LOV photoreceptor measured using kinetic quasi-elastic and elastic incoherent neutron scattering
Members of the LOV protein family are blue-light photoreceptors employing LOV domains as photosensory modules, controlling a number of cellular responses like phototropism, chloroplast movement, stomatal opening, regulation of circadian rhythms, photo-induced growth patterns and pigment synthesis. LOV domains are structurally well-conserved that typically bind a flavin chromophore. Upon light absorption, they undergo a covalent bond formation between the C4a atom of the flavin ring and the sulfur of the neighboring cysteine residue. The photocycle is thermally reversible and in the dark, the FMN-cysteinyl adduct decays to the ground state on a timescale of seconds to days. In this proposal we suggest to investigate changes of molecular dynamics through the dark recovery process of the photoreceptor PpSB1-LOV by experiments on IN16B and IN13. PpSB1-LOV has a dark recovery time of 39 h that enables kinetic QENS and EINS experiments. The aim of the experiments is to identify, if changes in molecular dynamics are directly linked to local rearrangements around the chromophore. Potentially we would also be able to identify transient intermediates that show different dynamics
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Andreas M. Stadler; KRAUSS Ulrich; NATALI Francesca; SARTER Mona and SEYDEL Tilo. (2018). Light-induced dynamics changes of a LOV photoreceptor measured using kinetic quasi-elastic and elastic incoherent neutron scattering. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-828
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