QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.

ABSTRACT: Photosensory receptors containing the flavin-binding light-oxygen-voltage (LOV) domain are modular proteins that fulfil a variety of biological functions ranging from gene expression to phototropism. The LOV photocycle is initiated by blue-light and involves a cascade of intermediate species, including an electronically excited triplet state, that leads to covalent bond formation between the flavin mononucleotide (FMN) chromophore and a nearby cysteine residue. Subsequent conformational changes in the polypeptide chain arise due to the remodelling of the hydrogen bond network in the cofactor binding pocket, whereby a conserved glutamine residue plays a key role in coupling FMN photochemistry with LOV photobiology. Although the dark-to-light transition of LOV photosensors has been previousl

SUBMITTER: Andrikopoulos PC 

PROVIDER: S-EPMC8246142 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature