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001     588
005     20200402205543.0
024 7 _ |2 pmid
|a pmid:18719097
024 7 _ |2 pmc
|a pmc:PMC2527874
024 7 _ |2 DOI
|a 10.1073/pnas.0802289105
024 7 _ |2 WOS
|a WOS:000258905700005
037 _ _ |a PreJuSER-588
041 _ _ |a eng
082 _ _ |a 000
084 _ _ |2 WoS
|a Multidisciplinary Sciences
100 1 _ |0 P:(DE-HGF)0
|a Jiang, X.
|b 0
245 _ _ |a Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy
260 _ _ |a Washington, DC
|b Academy
|c 2008
300 _ _ |a 12113 - 12117
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 5100
|a Proceedings of the National Academy of Sciences of the United States of America
|v 105
|x 0027-8424
|y 34
500 _ _ |a We 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.
520 _ _ |a Membrane 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.
536 _ _ |0 G:(DE-Juel1)FUEK409
|2 G:(DE-HGF)
|a Funktion und Dysfunktion des Nervensystems
|c P33
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Ion Channel Gating
650 _ 2 |2 MeSH
|a Light
650 _ 2 |2 MeSH
|a Membrane Potentials
650 _ 2 |2 MeSH
|a Membrane Proteins: chemistry
650 _ 2 |2 MeSH
|a Photoreceptor Cells: chemistry
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Rhodopsin: chemistry
650 _ 2 |2 MeSH
|a Spectrophotometry, Infrared: methods
650 _ 7 |0 0
|2 NLM Chemicals
|a Membrane Proteins
650 _ 7 |0 9009-81-8
|2 NLM Chemicals
|a Rhodopsin
650 _ 7 |2 WoSType
|a J
653 2 0 |2 Author
|a ion transfer
653 2 0 |2 Author
|a membrane potential
653 2 0 |2 Author
|a proton translocation
653 2 0 |2 Author
|a vibrational spectroscopy
653 2 0 |2 Author
|a sensory rhodopsin
700 1 _ |0 P:(DE-HGF)0
|a Zaitseva, E.
|b 1
700 1 _ |0 P:(DE-HGF)0
|a Schmidt, M.
|b 2
700 1 _ |0 P:(DE-HGF)0
|a Siebert, F.
|b 3
700 1 _ |0 P:(DE-HGF)0
|a Engelhard, M.
|b 4
700 1 _ |0 P:(DE-Juel1)VDB1421
|a Schlesinger, R.
|b 5
|u FZJ
700 1 _ |0 P:(DE-HGF)0
|a Ataka, K.
|b 6
700 1 _ |0 P:(DE-HGF)0
|a Vogel, R.
|b 7
700 1 _ |0 P:(DE-HGF)0
|a Heberle, J.
|b 8
773 _ _ |0 PERI:(DE-600)1461794-8
|a 10.1073/pnas.0802289105
|g Vol. 105, p. 12113 - 12117
|p 12113 - 12117
|q 105<12113 - 12117
|t Proceedings of the National Academy of Sciences of the United States of America
|v 105
|x 0027-8424
|y 2008
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2527874
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