ISIS Neutron and Muon Source Data Journal

Light-induced dynamics changes of a LOV photoreceptor investigated using time-resolved quasi-elastic neutron scattering

Abstract: 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 on a timescale of seconds to days. In this proposal, we suggest investigating changes of molecular dynamics through the dark recovery process of the photoreceptor PpSB1-LOV by time-resolved (TR) QENS experiments on IRIS after illumination of the photoreceptor in situ in the neutron beam. TR-QENS experiments are suggested to be performed as function of temperature to provide deeper insights into the kinetic mechanism.

Principal Investigator: Dr Andreas Stadler
Experimenter: Dr Julio Martín Pusterla
Experimenter: Dr Ulrich Krauss
Local Contact: Dr Mona Sarter

DOI: 10.5286/ISIS.E.RB2220017

ISIS Experiment Number: RB2220017

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Dr Andreas Stadler et al; (2024): Light-induced dynamics changes of a LOV photoreceptor investigated using time-resolved quasi-elastic neutron scattering, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB2220017

Data is released under the CC-BY-4.0 license.