The plant blue light receptor phototropin comprises a protein kinase domain and two FMN-binding LOV domains (LOV1 and LOV2).
First-pass extracted concept
FMN
Aliases
flavin mononucleotide, FMN chromophore
Evidence Snippets
Supporting Sources
Linked Claims
13C chemical shifts of FMN are differently modulated by complexation with the LOV domains studied, indicating slight differences in binding interactions between FMN and the apoproteins.
(13)C Chemical shifts of FMN are shown to be differently modulated by complexation with the LOV domains under study, indicating slight differences in the binding interactions of FMN and the apoproteins.
Using 13C NMR signal modulation after reconstitution with random libraries of 13C-labeled FMN isotopologues, all 13C signals of FMN bound to Avena sativa LOV1 and LOV2 and Adiantum capillus-veneris LOV2 were unequivocally assigned under dark and blue light conditions.
Using this approach, all (13)C signals of FMN bound to LOV1 and LOV2 domains of Avena sativa and to the LOV2 domain of the fern, Adiantum capillus-veneris, could be unequivocally assigned under dark and under blue light irradiation conditions.
Blue light irradiation of recombinant LOV domains promotes addition of a cysteinyl thiolate group to carbon 4a of the FMN chromophore, and spontaneous cleavage of that photoadduct completes the receptor photocycle.
Blue light irradiation of recombinant LOV domains is conducive to the addition of a cysteinyl thiolate group to carbon 4a of the FMN chromophore, and spontaneous cleavage of that photoadduct completes the photocycle of the receptor.
Phototropin comprises a protein kinase domain and two FMN-binding LOV domains, LOV1 and LOV2.
The plant blue light receptor phototropin comprises a protein kinase domain and two FMN-binding LOV domains (LOV1 and LOV2).