001     43304
005     20200423204004.0
024 7 _ |a pmid:15584756
|2 pmid
024 7 _ |a 10.1021/ja045951h
|2 DOI
024 7 _ |a WOS:000225697000055
|2 WOS
024 7 _ |a 2128/703
|2 Handle
037 _ _ |a PreJuSER-43304
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Chemistry, Multidisciplinary
100 1 _ |a Ataka, K.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB5396
245 _ _ |a Oriented attachment and membrane reconstitution of His-tagged cytochrome c oxidase to a gold electrode: in-situ monitoring by Surface Enhanced Infrared Absorption Spectroscopy
260 _ _ |a Washington, DC
|b American Chemical Society
|c 2004
300 _ _ |a 16199 - 16206
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 |a Journal of the American Chemical Society
|x 0002-7863
|0 8502
|v 126
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a A novel concept is introduced for the oriented incorporation of membrane proteins into solid supported lipid bilayers. Recombinant cytochrome c oxidase solubilized in detergent was immobilized on a chemically modified gold surface via the affinity of its histidine-tag to a nickel-chelating nitrilo-triacetic acid (NTA) surface. The oriented protein monolayer was reconstituted into the lipid environment by detergent substitution. The individual steps of the surface modification, including (1) chemical modification of the gold support, (2) adsorption of the protein, and (3) reconstitution of the lipid bilayer, were followed in situ by means of surface-enhanced infrared absorption spectroscopy (SEIRAS) and accompanied by normal-mode analysis. The high surface sensitivity of SEIRAS allows for the identification of each chemical reaction process within the monolayer at the molecular level. Finally, full functionality of the surface-tethered cytochrome c oxidase was demonstrated by cyclic voltammetry after binding of the natural electron donor cytochrome c.
536 _ _ |a Neurowissenschaften
|c L01
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Electrochemistry
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: chemistry
650 _ 2 |2 MeSH
|a Enzymes, Immobilized: chemistry
650 _ 2 |2 MeSH
|a Gold: chemistry
650 _ 2 |2 MeSH
|a Histidine: chemistry
650 _ 2 |2 MeSH
|a Lipid Bilayers: chemistry
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Nitrilotriacetic Acid: chemistry
650 _ 2 |2 MeSH
|a Recombinant Proteins: chemistry
650 _ 2 |2 MeSH
|a Spectroscopy, Fourier Transform Infrared: methods
650 _ 2 |2 MeSH
|a Surface Properties
650 _ 7 |0 0
|2 NLM Chemicals
|a Enzymes, Immobilized
650 _ 7 |0 0
|2 NLM Chemicals
|a Lipid Bilayers
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |0 139-13-9
|2 NLM Chemicals
|a Nitrilotriacetic Acid
650 _ 7 |0 71-00-1
|2 NLM Chemicals
|a Histidine
650 _ 7 |0 7440-57-5
|2 NLM Chemicals
|a Gold
650 _ 7 |0 EC 1.9.3.1
|2 NLM Chemicals
|a Electron Transport Complex IV
650 _ 7 |a J
|2 WoSType
700 1 _ |a Giess, F.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Knoll, W.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Naumann, R.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Haber-Pohlmeier, S.
|b 4
|u FZJ
|0 P:(DE-Juel1)VDB12272
700 1 _ |a Richter, B.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Heberle, J.
|b 6
|u FZJ
|0 P:(DE-Juel1)VDB572
773 _ _ |a 10.1021/ja045951h
|g Vol. 126, p. 16199 - 16206
|p 16199 - 16206
|q 126<16199 - 16206
|0 PERI:(DE-600)1472210-0
|t Journal of the American Chemical Society
|v 126
|y 2004
|x 0002-7863
856 7 _ |u http://dx.doi.org/10.1021/ja045951h
|u http://hdl.handle.net/2128/703
856 4 _ |u https://juser.fz-juelich.de/record/43304/files/60592.pdf
|y OpenAccess
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909 C O |o oai:juser.fz-juelich.de:43304
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913 1 _ |k L01
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914 1 _ |y 2004
915 _ _ |0 StatID:(DE-HGF)0010
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915 _ _ |2 StatID
|0 StatID:(DE-HGF)0510
|a OpenAccess
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
|x 0
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