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  The chromoprotein of halorhodopsin is the light-driven electrogenic chloride pump in Halobacterium halobium

Bamberg, E., Hegemann, P., & Oesterhelt, D. (1984). The chromoprotein of halorhodopsin is the light-driven electrogenic chloride pump in Halobacterium halobium. Biochemistry, 23(25), 6216-6221. doi:10.1021/bi00320a050.

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 Creators:
Bamberg, Ernst1, Author           
Hegemann, Peter2, Author
Oesterhelt, Dieter2, Author           
Affiliations:
1Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society, ou_3273415              
2Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565164              

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 Abstract: The chromoprotein of halorhodopsin was isolated from Halobacteriqm halobium strain L-33, a bacteriorhodopsin-deficient mutant, and incorporated into asolectin lipid vesicles. When these vesicles are added to one side ofa planar lipid membrane, the membrane system becomes photoelectrically active. The observed photoresponse occurs only in the presence of chloride (and other halides). The action spectrum of the photoresponse is identical with the visible absorption band of the chromoprotein in lipid vesicles. The photoresponse consists of a transient photocurrent, which indicates that the lipid vesicles are adsorbed to the surface of the planar lipid membrane but not integrated into it. The stationary photocurrent is extremely low because the underlyinglipid membrane is virtually impermeable to the transported ion. The stationary photocurrent, however, increases drastically upon the addition of the lipophilic anion tetraphenylborate or of the protonophore tetrachloro-2-(trifluoromethy1)benzimidazole (TTFB, HA) to the system. The TTFB-enhanced stationary photocurrent is caused by the transport of an HA2- species. The results obtained demonstrate that the chromoprotein of halorhodopsin is the lightdriven C1- pump in H. halobiurn.

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Language(s): eng - English
 Dates: 1984-03-282002-05-011984-12-04
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi00320a050
PMID: 24409552
 Degree: -

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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 23 (25) Sequence Number: - Start / End Page: 6216 - 6221 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103