bacteriorhodopsin


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bacteriorhodopsin

[bak‚tir·ē·ō·rō′däp·sən]
(biochemistry)
A purple substance in the cell membranes of halobacteria (found in extremely saline environments) during conditions of low oxygen, and consisting of the protein bacteriopsin and retinal, the same carotenoid found in the visual pigments of animals; in response to light, the purple membrane pumps protons out of the cell, providing the energy gradient for synthesis of adeniosine triphosphate.
References in periodicals archive ?
Honig, "Environmental effects on the protonation states of active site residues in bacteriorhodopsin," Biophysical Journal, vol.
Khorana, "The retinylidene Schiff base counterion in bacteriorhodopsin," Journal of Biological Chemistry, vol.
Bacteriorhodopsin is found in the intensely purple cell membrane of a bacterium called Halobacterium salinarium, which grows in salt marshes.
Walch, Bacteriorhodopsin Immobilized in Sol-Gel Glass.
Dencher, "Internal molecular motions of bacteriorhodopsin: hydration-induced flexibility studied by quasielastic incoherent neutron scattering using oriented purple membranes," National Academy of Sciences of the United States of America, vol.
Nonetheless, a primary example of a natural biomolecule exhibiting phase conjugation, even using low light intensities, is bacteriorhodopsin (Werner, 1990).
Halotolerance refers to some native adaptations including a highly saline cytoplasm, specialized salt-requiring proteins, and the unique light-driven proton as well as chloride pumps bacteriorhodopsin and halorhodopsin (4).
Mukohata, "ATP synthesis linked to light-dependent proton uptake in a red mutant strain of Halobacterium lacking bacteriorhodopsin," Archives of Biochemistry and Biophysics, vol.
The lipidic cubic phase method was developed by Rosenbusch and Landau, (125) and was used to crystalize bacteriorhodopsin. With the lipidic cubic phase method, membrane proteins are designed to be crystallized in the lipidic phase consisting of oleic acid instead of the aqueous phase.
Bredas, "The bacteriorhodopsin chromophore retinal and derivatives: an experimental and theoretical investigation of the second-order optical properties," Journal of the American Chemical Society, vol.
One bit of data could be stored by a single molecule of GFP rather than by macroscopic dots of bacteriorhodopsin, another light-responsive protein with data storage potential (SN: 3/8/97, p.