Light-induced changes of the proton affinities of amino acid side groups are the driving force
for proton translocation in bacteriorhodopsin. Recent progress in obtaining structures of …

A group of microbial retinal proteins most closely related to the proton pump
xanthorhodopsin has a novel sequence motif and a novel function. Instead of, or in addition …

A homologue of type I rhodopsin was found in the unicellular Gloeobacter violaceus
PCC7421, which is believed to be primitive because of the lack of thylakoids and peculiar …

Discovered over 50 years ago, bacteriorhodopsin is the first recognized and most widely
studied microbial retinal protein. Serving as a light-activated proton pump, it represents the …

We measured time-resolved difference spectra, in the visible and the infrared, for the Glu-
194 and Glu-204 mutants of bacteriorhodopsin and detected an anomalous O state, labeled …

Optogenetics relies on the expression of specific microbial rhodopsins in the neuronal
plasma membrane. Most notably, this includes channelrhodopsins, which when …

Channelrhodopsins (ChRs), which form a distinct branch of the microbial rhodopsin family,
control phototaxis in green algae. Because ChRs can be expressed and function in …

Similarly to bacteriorhodopsin, proteorhodopsin that normally contains all-trans and 13-cis
retinal is transformed at low pH to a species containing 9-cis retinal under continuous …

Microbial organisms utilize light not only as energy sources but also as signals by which
rhodopsins (containing retinal as a chromophore) work as photoreceptors. Sensory …

Retinylidene photoreceptors are ubiquitously present in marine protists as first documented
by the identification of green proteorhodopsin (GPR). We present a detailed investigation of …