Phytochromes are ubiquitous photoreceptors responsible for sensing light in plants, fungi
and bacteria. Their photoactivation is initiated by the photoisomerization of the embedded …

Bacteriophytochromes (BphPs) are photoreceptors that regulate a wide range of biological
mechanisms via red light–absorbing (Pr)–to–far-red light–absorbing (Pfr) reversible …

Photoactivation of bacteriophytochrome involves a cis–trans photoisomerization of a
biliverdin chromophore, but neither the precise sequence of events nor the direction of the …

Molecular switches alterable between two stable states by environmental stimuli, such as
light and temperature, offer the potential for controlling biological functions. Here, we report …

Phytochromes are red light-sensing photoreceptor proteins that bind a bilin chromophore.
Here, we investigate the role of a conserved histidine (H260) and tyrosine (Y263) in the …

Understanding photoisomerization dynamics in cyanobacteriochromes is important to the
development of optical agents in near-infrared biological imaging and optogenetics. Here …

Far-red cyanobacteriochromes (CBCRs) are bilin-based photosensory proteins that promise
to be novel optical agents in optogenetics and deep tissue imaging. Recent structural …

Cyanobacteriochromes (CBCRs) are promising optogenetic tools for their diverse
absorption properties with a single compact cofactor-binding domain. We previously …

We recently converted the GAF domain of NpR3784 cyanobacteriochrome into near‐
infrared (NIR) fluorescent proteins (FPs). Unlike cyanobacterichrome, which incorporates …

Using ultrafast spectroscopy and site-specific mutagenesis, we demonstrate the central role
of a conserved tyrosine within the chromophore binding pocket in the forward (P r→ P fr) …