Anion binding to the chloride pump, halorhodopsin, and its implications for the transport mechanism.
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.
Department of Physiology and Biophysics, University of California, Irvine 92717.
J K
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Lanyi
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Duschl
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Váro
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Zimányi
D001436:Bacteriorhodopsins / Q000378:metabolism*; D001693:Biological Transport, Active; D018118:Chloride Channels; D002712:Chlorides / Q000378:metabolism*; D006217:Halobacterium / Q000378:metabolism; D025602:Halorhodopsins; D007473:Ion Channels / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D009566:Nitrates / Q000378:metabolism
D018118:Chloride Channels; D002712:Chlorides; D025602:Halorhodopsins; D007473:Ion Channels; D008565:Membrane Proteins; D009566:Nitrates; D001436:Bacteriorhodopsins