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000000588 0247_ $$2DOI$$a10.1073/pnas.0802289105
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000000588 084__ $$2WoS$$aMultidisciplinary Sciences
000000588 1001_ $$0P:(DE-HGF)0$$aJiang, X.$$b0
000000588 245__ $$aResolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy
000000588 260__ $$aWashington, DC$$bAcademy$$c2008
000000588 300__ $$a12113 - 12117
000000588 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000000588 440_0 $$05100$$aProceedings of the National Academy of Sciences of the United States of America$$v105$$x0027-8424$$y34
000000588 500__ $$aWe thank Rebecca M. Nyquist for reading the manuscript; R.S. thanks Georg Buldt for generous support; and J.H. acknowledges helpful discussions with Eberhard Neumann and Benjamin Kaupp. This work was supported by grants from the German Ministry for Science and Education (to J.H.) and Deutsche Forschungsgemeinschaft Grant Vo 811/3,4 (to R.V.) and Za 566/1-1 (to E.Z.). X.J. thanks the Alexander-von-Humboldt foundation for a fellowship.
000000588 520__ $$aMembrane proteins are molecular machines that transport ions, solutes, or information across the cell membrane. Electrophysiological techniques have unraveled many functional aspects of ion channels but suffer from the lack of structural sensitivity. Here, we present spectroelectrochemical data on vibrational changes of membrane proteins derived from a single monolayer. For the seven-helical transmembrane protein sensory rhodopsin II, structural changes of the protein backbone and the retinal cofactor as well as single ion transfer events are resolved by surface-enhanced IR difference absorption spectroscopy (SEIDAS). Angular changes of bonds versus the membrane normal have been determined because SEIDAS monitors only those vibrations whose dipole moment are oriented perpendicular to the solid surface. The application of negative membrane potentials (DeltaV = -0.3 V) leads to the selective halt of the light-induced proton transfer at the stage of D75, the counter ion of the retinal Schiff base. It is inferred that the voltage raises the energy barrier of this particular proton-transfer reaction, rendering the energy deposited in the retinal by light excitation insufficient for charge transfer to occur. The other structural rearrangements that accompany light-induced activity of the membrane protein, are essentially unaffected by the transmembrane electric field. Our results demonstrate that SEIDAS is a generic approach to study processes that depend on the membrane potential, like those in voltage-gated ion channels and transporters, to elucidate the mechanism of ion transfer with unprecedented spatial sensitivity and temporal resolution.
000000588 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
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000000588 65320 $$2Author$$aion transfer
000000588 65320 $$2Author$$amembrane potential
000000588 65320 $$2Author$$aproton translocation
000000588 65320 $$2Author$$avibrational spectroscopy
000000588 65320 $$2Author$$asensory rhodopsin
000000588 650_2 $$2MeSH$$aIon Channel Gating
000000588 650_2 $$2MeSH$$aLight
000000588 650_2 $$2MeSH$$aMembrane Potentials
000000588 650_2 $$2MeSH$$aMembrane Proteins: chemistry
000000588 650_2 $$2MeSH$$aPhotoreceptor Cells: chemistry
000000588 650_2 $$2MeSH$$aProtein Conformation
000000588 650_2 $$2MeSH$$aRhodopsin: chemistry
000000588 650_2 $$2MeSH$$aSpectrophotometry, Infrared: methods
000000588 650_7 $$00$$2NLM Chemicals$$aMembrane Proteins
000000588 650_7 $$09009-81-8$$2NLM Chemicals$$aRhodopsin
000000588 650_7 $$2WoSType$$aJ
000000588 7001_ $$0P:(DE-HGF)0$$aZaitseva, E.$$b1
000000588 7001_ $$0P:(DE-HGF)0$$aSchmidt, M.$$b2
000000588 7001_ $$0P:(DE-HGF)0$$aSiebert, F.$$b3
000000588 7001_ $$0P:(DE-HGF)0$$aEngelhard, M.$$b4
000000588 7001_ $$0P:(DE-Juel1)VDB1421$$aSchlesinger, R.$$b5$$uFZJ
000000588 7001_ $$0P:(DE-HGF)0$$aAtaka, K.$$b6
000000588 7001_ $$0P:(DE-HGF)0$$aVogel, R.$$b7
000000588 7001_ $$0P:(DE-HGF)0$$aHeberle, J.$$b8
000000588 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.0802289105$$gVol. 105, p. 12113 - 12117$$p12113 - 12117$$q105<12113 - 12117$$tProceedings of the National Academy of Sciences of the United States of America$$v105$$x0027-8424$$y2008
000000588 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2527874
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