B0184
Bacteriorhodopsin from Halobacterium salinarum
native sequence, lyophilized powder
Synonym(s):
BR from H. salinarum, Bacterioopsin, Bacteriorhodopsin from Halobacterium halobium
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About This Item
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biological source
Halobacterium salinarium
Quality Level
form
lyophilized powder
technique(s)
ligand binding assay: suitable
mass spectrometry (MS): suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
Halobacterium salinarium ... OE_RS05715(5953595) , VNG_RS05715(144807)
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General description
Bacteriorhodopsin (BR) is a covalent complex comprising bacterioopsin protein and retinal cofactor in the equimolar ratio. It corresponds to the molecular weight of 27kDa. BR belongs to the retinylidene class of proteins. It is a seven-membrane helical protein that acts as a photon-driven pump. BR can be used in studies of the folding and kenetics of β-helical proteins.
Bacteriorhodopsin is the prototypical "seven-helix" transmembrane protein (with seven α-helical domains), whose study led to advances in understanding G protein-coupled receptors (GPCRs). In Halobacteria, it acts as a light-harvesting protein, producing a proton gradient across the cell wall that is then used to drive biosynthetic processes.
Application
Bacteriorhodopsin from Halobacterium salinarum has been used:
- in generation of droplet lipid bilayer
- as a standard in quadrupole time-of-flight (QTOF) mass spectroscopy (MS)
- in the generation of protein-detergent complex and micelles for dynamic light scattering studies
Bacteriorhodopsin is of interest in the development of artificial retinas, optical associative processors, and three-dimensional memory storage devices.
Biochem/physiol Actions
Bacteriorhodopsin (BR) from Halobacterium salinarum acts as a proton-driven pump. BR can be used in studies of the folding and kinetics of α-helical proteins. It is thermally stable and exhibits high photoelectric and photochemical efficiency. BR exists as trimer in a hexagonal lattice. Its photocycle intermediates are exploited in bioelectronics majorly in photoelectric and photochemical applications.
A transmembrane retinylidine protein that functions as a proton pump driven by light energy in Holobacterium.
Preparation Note
Aqueous suspensions may be sonicated to achieve the desired homogeneity and may be stored for a short time at a temperature of 2-8 °C or at a temperature of -20 °C without time limitation.
Wild-type bacteriorhodopsin is isolated from Halobacterium salinarum strain S9 as purple membranes.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Light-Patterned Current Generation in a Droplet Bilayer Array
Schild V, et al.
Scientific reports, 7, 46585-46585 (2017)
Alice Dimonte et al.
Biomacromolecules, 13(11), 3503-3509 (2012-10-11)
Molecular nanoelectronics is attracting much attention, because of the possibility to add functionalities to silicon-based electronics by means of intrinsically nanoscale biological or organic materials. The contact point between active molecules and electrodes must present, besides nanoscale size, a very
Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in Halobacterium salinarum
Dummer AM, et al.
Journal of Bacteriology, 193(20), 5658-5667 (2011)
Systematic analysis of protein-detergent complexes applying dynamic light scattering to optimize solutions for crystallization trials
Meyer A, et al.
Acta Crystallographica. Section F, Structural Biology Communications, 71(1), 75-81 (2015)
Light-independent phospholipid scramblase activity of bacteriorhodopsin from Halobacterium salinarum
Verchere A, et al.
Scientific reports, 7(1), 9522-9522 (2017)
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