Infrared difference spectroscopy probes vibrational changes of proteins upon their
perturbation. Compared with other spectroscopic methods, it stands out by its sensitivity to …

Red and far-red light–sensing phytochromes are widespread in nature, occurring in plants,
algae, fungi, and prokaryotes. Despite at least a billion years of evolution, their photosensory …

Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi,
and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to …

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

The orange carotenoid protein (OCP) is a two-domain photoactive protein that noncovalently
binds an echinenone (ECN) carotenoid and mediates photoprotection in cyanobacteria. In …

Phytochromes are ubiquitous photoreceptor proteins that undergo a significant refolding of
secondary structure in response to initial photoisomerization of the chromophoric group …

Phytochromes are ubiquitous photosensor proteins, which control the growth, reproduction
and movement in plants, fungi and bacteria. Phytochromes switch between two …

The biological function of phytochromes is triggered by an ultrafast photoisomerization of the
tetrapyrrole chromophore biliverdin between two rings denoted C and D. The mechanism by …

Highlights•Fluorescent probes or optogenetic tools can be developed using phytochrome
modules.•Bacteriophytochromes provide advantageous properties in protein engineering …

Phytochromes belong to a group of photoreceptor proteins containing a covalently bound
biliverdin chromophore that inter-converts between two isomeric forms upon photoexcitation …