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 …

Flavins have emerged as central to electron bifurcation, signaling, and countless enzymatic
reactions. In bifurcation, two electrons acquired as a pair are separated in coupled transfers …

Photoactivated adenylate cyclases (PACs) are light-activated enzymes that combine a BLUF
(blue-light using flavin) domain and an adenylate cyclase domain that are able to increase …

The structural dynamics following photoexcitation of a photosensing BLUF (blue light
sensing using FAD) domain protein have been investigated by ultrafast transient infrared …

A novel flavin-dipicolylamine conjugate was designed for highly selective and sequential
recognition of zinc and phosphate ions based on OFF-ON-OFF mode of detection. While …

Phototropins, major blue-light receptors in plants, are sensitive to blue light through a pair of
flavin mononucleotide (FMN)-binding light oxygen and voltage (LOV) domains, LOV1 and …

BLUF domains constitute a recently discovered class of photoreceptor proteins found in
bacteria and eukaryotic algae. BLUF domains are blue-light sensitive through a FAD …

Living systems are fundamentally dependent on the ability of proteins to respond to external
stimuli. The mechanism, the underlying structural dynamics, and the time scales for …

Combined studies on fluorescence quantum yield of coenzymes NADH and FAD in water–
methanol, water–ethanol and water–propylene glycol mixtures and on time-resolved …

The pH dependent behavior of two flavin cofactors, flavin-adenine dinucleotide (FAD) and
flavin mononucleotide (FMN), has been characterized using femtosecond transient …