Proteorhodopsins are the most abundant retinal based photoreceptors and their phototrophic function might be relevant in marine ecosystems. Here, we describe their remarkable molecular properties with a special focus on the green absorbing variant. Its distinct features include a high pK<sub>a</sub> value of the primary proton acceptor stabilized through an interaction with a conserved histidine, a long-range interaction between the cytoplasmic EF loop and the chromophore entailing a particularmode of color tuning and a variable proton pumping vectoriality with complex voltage-dependence. The proteorhodopsin family represents a profound example for structure–function relationships. Especially the development of a biophysical understanding o...
Retinylidene photoreceptors are ubiquitously present in marine protists as first documented by the i...
AbstractProteorhodopsin (PR), a retinal-containing seven transmembrane helix protein, functions as a...
The photophysical properties of the retinal-binding proteins, rhodopsin, bacteriorhodopsin and selec...
Proteorhodopsins are the most abundant retinal based photoreceptors and their phototrophic function ...
AbstractProteorhodopsins are the most abundant retinal based photoreceptors and their phototrophic f...
Proteorhodopsins are heptahelical membrane proteins which function as light-driven proton pumps. The...
Proteorhodopsin, a homologue of archaeal bacteriorhodopsin (BR), belongs to a newly identified famil...
Proteorhodopsins are heptahelical membrane proteins which function as light-driven proton pumps. The...
Proteorhodopsin, a homologue of archaeal bacteriorhodopsin (BR), belongs to a newly identified famil...
AbstractProteorhodopsin is a family of over 50 proteins that provide phototrophic capability to mari...
The proteorhodopsin family consists of hundreds of homologous retinal containing membrane proteins f...
ABSTRACT: The absorption spectrum of green proteorhodopsin (GPR) is pH-dependent, exhibiting either ...
Retinylidene photoreceptors are ubiquitously present in marine protists as first documented by the i...
Proteorhodopsins (PRs) found in marine microbes are the most abundant retinal-based photoreceptors o...
Proteorhodopsin (PR) is a light-driven proton pump found in marine bacteria. Thousands of PRs are cl...
Retinylidene photoreceptors are ubiquitously present in marine protists as first documented by the i...
AbstractProteorhodopsin (PR), a retinal-containing seven transmembrane helix protein, functions as a...
The photophysical properties of the retinal-binding proteins, rhodopsin, bacteriorhodopsin and selec...
Proteorhodopsins are the most abundant retinal based photoreceptors and their phototrophic function ...
AbstractProteorhodopsins are the most abundant retinal based photoreceptors and their phototrophic f...
Proteorhodopsins are heptahelical membrane proteins which function as light-driven proton pumps. The...
Proteorhodopsin, a homologue of archaeal bacteriorhodopsin (BR), belongs to a newly identified famil...
Proteorhodopsins are heptahelical membrane proteins which function as light-driven proton pumps. The...
Proteorhodopsin, a homologue of archaeal bacteriorhodopsin (BR), belongs to a newly identified famil...
AbstractProteorhodopsin is a family of over 50 proteins that provide phototrophic capability to mari...
The proteorhodopsin family consists of hundreds of homologous retinal containing membrane proteins f...
ABSTRACT: The absorption spectrum of green proteorhodopsin (GPR) is pH-dependent, exhibiting either ...
Retinylidene photoreceptors are ubiquitously present in marine protists as first documented by the i...
Proteorhodopsins (PRs) found in marine microbes are the most abundant retinal-based photoreceptors o...
Proteorhodopsin (PR) is a light-driven proton pump found in marine bacteria. Thousands of PRs are cl...
Retinylidene photoreceptors are ubiquitously present in marine protists as first documented by the i...
AbstractProteorhodopsin (PR), a retinal-containing seven transmembrane helix protein, functions as a...
The photophysical properties of the retinal-binding proteins, rhodopsin, bacteriorhodopsin and selec...