The first member and eponym of the rhodopsin family was identified in the 1930s as the
visual pigment of the rod photoreceptor cell in the animal retina. It was found to be a …

The wild type green fluorescent protein (GFP) from Aequorea victoria has been extensively
investigated with a strong focus on the photochemistry and structural dynamics that are …

All‐trans to 13‐cis photoisomerization of the protonated retinal Schiff base (PRSB)
chromophore is the primary step that triggers various biological functions of microbial …

The primary reaction dynamics of channelrhodopsin-2 was investigated using femtosecond
vis-pump/mid-IR probe spectroscopy. Due to the fast deactivation of the excited state in …

Photochemistry in retinal proteins (RPs) is determined both by the properties of the retinal
chromophore and by its interactions with the surrounding protein. The initial retinal …

The primary stages of the Exiguobacterium sibiricum rhodopsin (ESR) photocycle were
investigated by femtosecond absorption laser spectroscopy in the spectral range of 400–900 …

Proteorhodopsins are an extensive family of photoactive membrane proteins found in
proteobacteria distributed throughout the world's oceans which are often classified as green …

Ultrafast transient absorption spectroscopy of wild-type bacteriorhodopsin (WT bR) and 2
tryptophan mutants (W86F and W182F) is performed with visible light excitation (pump) and …

We present a comparative study using femtosecond pump/probe spectroscopy in the visible
and infrared of the early photodynamics of solubilized proteorhodopsin (green absorbing …

Proteorhodopsin is an ion-translocating member of the microbial rhodopsin family. Light
absorption by its retinal chromophore initiates a photocycle, driven by trans/cis …