Following the formation kinetics of a transient intermediate of a photoreceptor during its photocycle with time-resolved QENS
Members of the LOV protein family are blue-light photoreceptors employing LOV domains as photosensory modules. 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. In this proposal we suggest to investigate changes of molecular dynamics through the dark recovery process of the photoreceptor PpSB1-LOV by QENS experiments on IN16B. In a previous experiment on IN16B we found a transient intermediate during the dark-recovery process that is formed with a kinetic relaxation time of 11 h. That intermediate has different dynamic behaviour than the light-excited state and comparatively similar dynamic behaviour as the fully dark-adapted ground state that is formed with significantly slower relaxation time of 39h. In the present proposal we would like to use elastic & inelastic fixed-windows scans to observe initial dynamical changes and to identify dynamical transitions more rapidly.
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The recommended format for citing this dataset in a research publication is in the following format:
Andreas M. Stadler; GRAF VON WESTARP Igor; HARIS Luman; KRAUSS Ulrich; SARTER Mona and SEYDEL Tilo. (2021). Following the formation kinetics of a transient intermediate of a photoreceptor during its photocycle with time-resolved QENS. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-887
This data is not yet public
This data is not yet public
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