Results 181 to 190 of about 3,121 (204)
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Cation Binding to Halorhodopsin
Biochemistry, 2015A member of the retinal protein family, halorhodopsin, acts as an inward light-driven Cl(-) pump. It was recently demonstrated that the Natronomonas pharaonis halorhodopsin-overproducing mutant strain KM-1 contains, in addition to the retinal chromophore, a lipid soluble chromophore, bacterioruberin, which binds to crevices between adjacent protein ...
Sansa, Dutta +2 more
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Microbial Halorhodopsins: Light-Driven Chloride Pumps
Chemical Reviews, 2018Early research on the four microbial rhodopsins discovered in the archaeal Halobacterium salinarum revealed a structural template that served as a scaffold for two different functions: light-driven ion transport and phototaxis. Bacteriorhodopsin and halorhodopsin are proton and chloride pumps, respectively, while sensory rhodopsin I and II are ...
Christopher Engelhard +3 more
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Light and dark adaptation of halorhodopsin
Archives of Biochemistry and Biophysics, 1985Dark incubation of envelope vesicles derived from a strain of Halobacterium halobium that lacks bacteriorhodopsin but contains halorhodopsin and a third rhodopsin-like pigment caused a decrease in the flash yield [the amplitude of a transient absorbance change of flash reactive component(s) by flash] of halorhodopsin but not the rhodopsin-like pigment.
N, Kamo +3 more
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Photochemistry of Halorhodopsin
2015Halorhodopsin is a light-driven inward Cl− pump found in the membrane of a halophilic archaeon called Halobacterium salinarum. While the physiological role of halorhodopsin has not been fully resolved, its functional mechanism has been studied as a model system for anion transport.
Takashi Kikukawa +2 more
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Crystallization of Halorhodopsin from Halobacterium sp. shark
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2005The chloride-ion-pumping channel, halorhodopsin from Halobacterium sp. shark was detergent-solubilized and 3-D crystallized. Proteins were solubilized using the nonionic detergent n-octyl-beta-D-glucoside and were crystallized as thin-plate crystals with polyethylene glycol 4000 as a precipitant.
Hirokazu, Nishida +3 more
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Bacteriorhodopsin and halorhodopsin: Multiple ion pumps
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1990Des membranes pourpres d'Halobacterium halobium contenant la bacteriorhodopsine ont ete soumis a des pulses laser ou a une irradiation continue en lumiere visible. En fonction du pH, la capacite et la specificite du transport d'ions par la bacteriorhodopsine et l'halorhodopsine sont ...
L. Keszthelyi +3 more
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Halorhodopsin: A Light-Driven Chloride Ion Pump
Annual Review of Biophysics and Biomolecular Structure, 1986Studies of bacteriorhodopsin over the past fourteen years have contributed in a special special way to our present understanding of ionic pumps and membrane proteins in general. This is because bacteriorhodopsin, a light driven proton pump found in the halo bacteria, is a small membrane protein that contains the minimum features required for active ...
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Anion selectivity and pumping mechanism of halorhodopsin
Biophysical Chemistry, 1995Comparison of the amino acid sequences in the A-B and B-C interhelical loop segments in all bacteriorhodopsins and halorhodopsins has shed light on the anion selectivity and pumping mechanism of halorhodopsin. The nucleotide sequences of two haloopsins from two new halobacterial strains, shark and port, have been determined, and shark halorhodopsin was
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Spectral Tuning in Halorhodopsin: The Chloride Pump Photoreceptor
Journal of the American Chemical Society, 2013The spectral tuning of halorhodopsin from Halobacterium salinarum (shR) during anion transport was analyzed at the molecular level using DFT-QM/MM [SORCI+Q//B3LYP/6-31G(d):Amber96] hybrid methods. Insights into the influence of Cl(-) depletion, Cl(-) substitution by N3(-) or NO3(-), and mutation of key amino acid residues along the ion translocation ...
Rhitankar, Pal +2 more
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Structure and Function of Halorhodopsin
Israel Journal of Chemistry, 1995AbstractA comprehensive review of the physiology, structure, and function of halorhodopsin (HR), the only known light‐driven anion pump, is presented. Beside the well‐studied transport function of HR in intact cells the article focuses on recent results about the molecular properties of HR.
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