Three major classes of flavin photosensors, light oxygen voltage (LOV) domains, blue light
sensor using FAD (BLUF) proteins and cryptochromes (CRYs), regulate diverse biological …

Conspectus Light activated proteins are at the heart of photobiology and optogenetics, so
there is wide interest in understanding the mechanisms coupling optical excitation to protein …

The hydrogen bonding network that surrounds the flavin in blue light using flavin adenine
dinucleotide (BLUF) photoreceptors plays a crucial role in sensing and communicating the …

Proton-coupled electron transfer (PCET) is key to the activation of the blue light using flavin
(BLUF) domain photoreceptors. Here, to elucidate the photocycle of the central FMN-Gln-Tyr …

The first stage in biological signaling is based on changes in the functional state of a
receptor protein triggered by interaction of the receptor with its ligand (s). The light-triggered …

Blue light using flavin (BLUF) photoreceptors respond to light via one of nature's smallest
photo-switching domains. Upon photo-activation, the flavin cofactor in the BLUF domain …

Photoreceptor proteins have been used to study how protein conformational changes are
induced by alterations in their environments and how their signals are transmitted to …

Molecules with conjugated π systems often feature strong electron correlation and therefore
require multireference methods for a reliable computational description. A key prerequisite …

Blue light using flavin (BLUF) photoreceptor proteins are critical for many light-activated
biological processes and are promising candidates for optogenetics because of their …

The flavin chromophore in blue-light-using FAD (BLUF) photoreceptors is surrounded by a
hydrogen bond network that senses and responds to changes in the electronic structure of …