%0 Journal Article
%A Röllen, Katrin
%A Granzin, Joachim
%A Batra-Safferling, Renu
%A Stadler, Andreas Maximilian
%T Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein
%J PLoS one
%V 13
%N 7
%@ 1932-6203
%C Lawrence, Kan.
%I PLoS
%M FZJ-2018-04635
%P e0200746
%D 2018
%X Light, oxygen, voltage (LOV) photoreceptors consist of conserved photo-responsive domains in bacteria, archaea, plants and fungi, and detect blue-light via a flavin cofactor. We investigated the blue-light induced conformational transition of the dimeric photoreceptor PpSB1-LOV-R66I from Pseudomonas putida in solution by using small-angle X-ray scattering (SAXS). SAXS experiments of the fully populated light- and dark-states under steady-state conditions revealed significant structural differences between the two states that are in agreement with the known structures determined by crystallography. We followed the transition from the light- to the dark-state by using SAXS measurements in real-time. A two-state model based on the light- and dark-state conformations could describe the measured time-course SAXS data with a relaxation time τREC of ~ 34 to 35 min being larger than the recovery time found with UV/vis spectroscopy. Unlike the flavin chromophore-based UV/vis method that is sensitive to the local chromophore environment in flavoproteins, SAXS-based assay depends on protein conformational changes and provides with an alternative to measure the recovery kinetics.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:30011332
%U <Go to ISI:>//WOS:000438829800048
%R 10.1371/journal.pone.0200746
%U https://juser.fz-juelich.de/record/850884