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Bacteriorhodopsin from Halobacterium salinarum

native sequence, lyophilized powder

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Synonym(s):
BR from H. salinarum, Bacterioopsin, Bacteriorhodopsin from Halobacterium halobium
CAS Number:
MDL number:
NACRES:
NA.56

biological source

Halobacterium salinarium

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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Bovine Serum Albumin lyophilized powder, protease, essentially free, ≥98% (agarose gel electrophoresis)

Sigma-Aldrich

A4737

Bovine Serum Albumin

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

technique(s)

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

technique(s)

activity assay: suitable

technique(s)

ligand binding assay: suitable

technique(s)

HPLC: suitable, MALDI-MS: suitable

UniProt accession no.

B0R5N9

UniProt accession no.

P00738

UniProt accession no.

P02769

UniProt accession no.

Q58D62

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

100

Quality Level

200

Quality Level

200

Quality Level

200

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

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Katia March et al.
Journal of microscopy, 282(3), 215-223 (2020-12-12)
Infrared spectroscopy is a powerful technique for characterising protein structure. It is now possible to record energy losses corresponding to the infrared region in the electron microscope and to avoid damage by positioning the probe in the region adjacent to
Light-independent phospholipid scramblase activity of bacteriorhodopsin from Halobacterium salinarum
Verchere A, et al.
Scientific reports, 7(1), 9522-9522 (2017)
Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding
Curnow P and Booth PJ
Proceedings of the National Academy of Sciences of the USA, 104(48), 18970-18975 (2007)
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)
Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in Halobacterium salinarum
Dummer AM, et al.
Journal of Bacteriology, 193(20), 5658-5667 (2011)

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