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B0184

Sigma-Aldrich

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

CAS Number:
53026-44-1
MDL number:
MFCD00130599
UNSPSC Code:
12352202
NACRES:
NA.56

biological source

Halobacterium salinarium

form

lyophilized powder

technique(s)

ligand binding assay: suitable
mass spectrometry (MS): suitable

UniProt accession no.

B0R5N9

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A review on bacteriorhodopsin-based bioelectronic devices
Li YT, et al.
Sensors, 18(5), 1368-1368 (2018)
High production of bacteriorhodopsin from wild type Halobacterium salinarum
Seyedkarimi MS, et al.
Extremophiles : Life Under Extreme Conditions, 19(5), 1021-1028 (2015)
Jonathan P Schlebach et al.
Protein science : a publication of the Protein Society, 21(1), 97-106 (2011-11-19)
The elucidation of the physical principles that govern the folding and stability of membrane proteins is one of the greatest challenges in protein science. Several insights into the folding of α-helical membrane proteins have come from the investigation of the
Light-Patterned Current Generation in a Droplet Bilayer Array
Schild V, et al.
Scientific reports, 7, 46585-46585 (2017)
Best practices and benchmarks for intact protein analysis for top-down mass spectrometry
Donnelly DP, et al,
Nature Methods, 16(7), 587-594 (2019)
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