Results 191 to 200 of about 3,121 (204)

Modeling of halorhodopsin and rhodopsin based on bacteriorhodopsin

Proteins: Structure, Function, and Genetics, 1996
Bacteriorhodopsin (BR), halorhodopsin (HR), and rhodopsin (Rh) all belong to the class of seven-helix membrane proteins. For BR, a structural model at atomic resolution is available; for HR, diffraction data are available only down to a resolution of 6 A in the membrane plane, and for Rh, down to 9 A.
M, Neumüller, F, Jähnig
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Blue Halorhodopsin from Natronobacterium pharaonis: Wavelength Regulation by Anions

Biochemistry, 1994
Halorhodopsin, the chloride pump from Natronobacterium pharaonis (pharaonis hR), was isolated under conditions of low ionic strength. The quotient between the optical densities of pharaonis hR in 4 M NaCl at 280 and 577 nm amounts to 1.1, indicating a high purity of the protein and integrity of the chromophore.
B, Scharf, M, Engelhard
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Nature of the principal photointermediate of halorhodopsin

Biochemical and Biophysical Research Communications, 1984
Two alternative hypotheses have been presented as to the nature of the principal halorhodopsin photointermediate: a) it is a form whose its absorption band is shifted from the 575 nm position to 500 or 520 nm, and b) it is a form whose absorption band is shifted to only about 565 nm, but with an altered band shape so it exhibits a fortuitous difference
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Photoelectric response of halorhodopsin from Natronobacterium pharaonis

Bioelectrochemistry and Bioenergetics, 1998
Abstract Halorhodopsin (hR) is an inward-directed light-driven chloride pump. This protein, from Natronobacterium pharaonis (abbreviated by phR), was immobilized on a transparent SnO 2 electrode to construct a sandwich-type electrochemical cell.
Koichi Koyama, Masato Sumi, Naoki Kamo, Janos K Lanyi   +3 more
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Halorhodopsin, a light-driven electrogenic chloride-transport system

Physiological Reviews, 1990
Cet expose resume les decouvertes concernant les halorhodopsines qui ont un rapport avec le transport ionique et en particulier le transport du ...
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Absorption spectral properties of purified halorhodopsin.

Journal of biochemistry, 1984
Halorhodopsin in the membrane fragments of Halobacterium halobium Y1 showed an absorption band at 576 nm, the intensity of which decreased on irradiation with red light at 0 degrees C (Ogurusu, T., Maeda, A., Sasaki, N., & Yoshizawa, T. (1981) J. Biochem. 90, 1267-1273). Using this photobleachable property as the basis for an assay of halorhodopsin, we
T, Ogurusu, A, Maeda, T, Yoshizawa
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Mechanism of base-catalyzed Schiff base deprotonation in halorhodopsin

Biochemistry, 1986
It has been shown earlier that the deprotonation of the Schiff base of illuminated halorhodopsin proceeds with a much lower pKa than that of the unilluminated pigment and the reversible protonation change is catalyzed by azide and cyanate [Hegemann, P., Oesterhelt, D., & Steiner, M. (1985) EMBO J. 4, 2347-2350].
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Characterization of Halorhodopsin reconstituted in asolectin liposomes

1988
The transport activity of the light-driven chloride pump halorhodopsin incorporated in asolectin vesicles was characterized using the passive proton movement as an indicator for the primary transport. Optimized conditions could be found for this reconstitution system.
M. Beckmann, J. Tittor, D. Oesterhelt
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Mechanism of Chloride Transport by Halorhodopsin

1988
The halobacterial retinal protein HR, which functions as a light-driven electrogenic chloride pump, is a small integral membrane protein, which undergoes various photoreactions including rapid cyclic isomerisation of the retinal from all-trans to 13-cis.
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Halorhodopsin: light-driven ion pumping made simple?

Current Opinion in Structural Biology, 2002
Halorhodopsin, a light-driven halide pump, is the second archaeal rhodopsin involved in ion pumping to be studied at high resolution by X-ray crystallography. Like its cousin bacteriorhodopsin, halorhodopsin couples vectorial ion transport to the isomerisation state of a covalently linked retinal.
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