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000043304 0247_ $$2DOI$$a10.1021/ja045951h
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000043304 084__ $$2WoS$$aChemistry, Multidisciplinary
000043304 1001_ $$0P:(DE-Juel1)VDB5396$$aAtaka, K.$$b0$$uFZJ
000043304 245__ $$aOriented attachment and membrane reconstitution of His-tagged cytochrome c oxidase to a gold electrode: in-situ monitoring by Surface Enhanced Infrared Absorption Spectroscopy
000043304 260__ $$aWashington, DC$$bAmerican Chemical Society$$c2004
000043304 300__ $$a16199 - 16206
000043304 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000043304 440_0 $$08502$$aJournal of the American Chemical Society$$v126$$x0002-7863
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000043304 520__ $$aA novel concept is introduced for the oriented incorporation of membrane proteins into solid supported lipid bilayers. Recombinant cytochrome c oxidase solubilized in detergent was immobilized on a chemically modified gold surface via the affinity of its histidine-tag to a nickel-chelating nitrilo-triacetic acid (NTA) surface. The oriented protein monolayer was reconstituted into the lipid environment by detergent substitution. The individual steps of the surface modification, including (1) chemical modification of the gold support, (2) adsorption of the protein, and (3) reconstitution of the lipid bilayer, were followed in situ by means of surface-enhanced infrared absorption spectroscopy (SEIRAS) and accompanied by normal-mode analysis. The high surface sensitivity of SEIRAS allows for the identification of each chemical reaction process within the monolayer at the molecular level. Finally, full functionality of the surface-tethered cytochrome c oxidase was demonstrated by cyclic voltammetry after binding of the natural electron donor cytochrome c.
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000043304 650_2 $$2MeSH$$aElectrochemistry
000043304 650_2 $$2MeSH$$aElectron Transport Complex IV: chemistry
000043304 650_2 $$2MeSH$$aEnzymes, Immobilized: chemistry
000043304 650_2 $$2MeSH$$aGold: chemistry
000043304 650_2 $$2MeSH$$aHistidine: chemistry
000043304 650_2 $$2MeSH$$aLipid Bilayers: chemistry
000043304 650_2 $$2MeSH$$aModels, Molecular
000043304 650_2 $$2MeSH$$aNitrilotriacetic Acid: chemistry
000043304 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000043304 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared: methods
000043304 650_2 $$2MeSH$$aSurface Properties
000043304 650_7 $$00$$2NLM Chemicals$$aEnzymes, Immobilized
000043304 650_7 $$00$$2NLM Chemicals$$aLipid Bilayers
000043304 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000043304 650_7 $$0139-13-9$$2NLM Chemicals$$aNitrilotriacetic Acid
000043304 650_7 $$071-00-1$$2NLM Chemicals$$aHistidine
000043304 650_7 $$07440-57-5$$2NLM Chemicals$$aGold
000043304 650_7 $$0EC 1.9.3.1$$2NLM Chemicals$$aElectron Transport Complex IV
000043304 650_7 $$2WoSType$$aJ
000043304 7001_ $$0P:(DE-HGF)0$$aGiess, F.$$b1
000043304 7001_ $$0P:(DE-HGF)0$$aKnoll, W.$$b2
000043304 7001_ $$0P:(DE-HGF)0$$aNaumann, R.$$b3
000043304 7001_ $$0P:(DE-Juel1)VDB12272$$aHaber-Pohlmeier, S.$$b4$$uFZJ
000043304 7001_ $$0P:(DE-HGF)0$$aRichter, B.$$b5
000043304 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b6$$uFZJ
000043304 773__ $$0PERI:(DE-600)1472210-0$$a10.1021/ja045951h$$gVol. 126, p. 16199 - 16206$$p16199 - 16206$$q126<16199 - 16206$$tJournal of the American Chemical Society$$v126$$x0002-7863$$y2004
000043304 8567_ $$uhttp://hdl.handle.net/2128/703$$uhttp://dx.doi.org/10.1021/ja045951h
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