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Reconstitution of the light-driven electrogenic ion pump halorhodopsin in black lipid membranes

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Bamberg,  Ernst
Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society;

Hegemann,  Peter
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Oesterhelt,  Dieter
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Bamberg, E., Hegemann, P., & Oesterhelt, D. (1984). Reconstitution of the light-driven electrogenic ion pump halorhodopsin in black lipid membranes. Biochimica et Biophysica Acta-Biomembranes, 773(1), 53-60. doi:10.1016/0005-2736(84)90549-2.


Cite as: http://hdl.handle.net/21.11116/0000-0007-A65E-5
Abstract
Halorhodopsin-containing membrane fragments were isolated from Halobacterium halobium strain L-33, a bacteriorhodopsin-deficient mutant. When these so called Tween-washed membrane fragments are added to one side of a positively charged planar lipid bilayer the system becomes photoelectrically active. Under stationary light conditions photocurrent transients are obtained while the steady-state photocurrent is extremely low. The steady-state photocurrent, however, is considerably increased when the lipid bilayer is doped with the Cl/OH exchanging carrier triphenyltin together with a proton carrier. These results suggest that halorhodopsin is associated with the underlying black lipid membrane in a sandwich-like structure. The photoresponse occurs only in the presence of Cl, Br and I with half-saturation concentrations in the range of 1–10 mM and is virtually independent on the type of the cation (Na+, K+, Mg2+) present. With other anions, such as SO4−2, Fand NO3 no photoresponse was obtained. The results provide direct evidence that halorhodopsin is a light-driven electrogenic pump with a high specificity for halides.