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PMID: 1694779 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Anion binding to the chloride pump, halorhodopsin, and its implications for the transport mechanism.

FEBS letters ·Vol. 265 ·No. 1-2 ·1990-06-04 ·Pages 1-6

Lanyi JK, Duschl A, Váro G, Zimányi L

Abstract

The light-driven chloride pump, halorhodopsin, binds and transports chloride across the membrane, and to a lesser extent nitrate. Binding and transport kinetics, and resonance Raman spectra of the retinal Schiff base, with these anions suggest the existence of two mutually exclusive binding sites. One of these may be the uptake site, and the other the release site during the transport. Plausible locations can be suggested for these sites, because halorhodopsin is a small protein with few buried positively charged residues, and the primary structure of a second pigment with similar function has recently become available for comparison.

MeSH Terms
Bacteriorhodopsins/metabolism Biological Transport, Active Chloride Channels Chlorides/metabolism Halobacterium/metabolism Halorhodopsins Ion Channels/metabolism Membrane Proteins/metabolism Nitrates/metabolism
Chemicals
Chloride Channels Chlorides Halorhodopsins Ion Channels Membrane Proteins Nitrates Bacteriorhodopsins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Lanyi J K
Department of Physiology and Biophysics, University of California, Irvine 92717.
Duschl A
Váro G
Zimányi L
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1990-06-04
Pages
1-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NIGMS NIH HHS · GM 29498 · United States
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