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000047540 084__ $$2WoS$$aChemistry, Multidisciplinary
000047540 084__ $$2WoS$$aChemistry, Physical
000047540 084__ $$2WoS$$aMaterials Science, Multidisciplinary
000047540 1001_ $$0P:(DE-Juel1)128707$$aMayer, D.$$b0$$uFZJ
000047540 245__ $$aScanning Probe Microscopic Studies of the Oriented Attachment and Membrane Reconstitution of Cytochrome c Oxidase to a Gold Electrode
000047540 260__ $$aWashington, DC$$bACS Publ.$$c2005
000047540 300__ $$a8580 - 8583
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000047540 440_0 $$04081$$aLangmuir$$v21$$x0743-7463
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000047540 520__ $$aScanning probe microscopy was used to monitor the resulting surface of the oriented incorporation of cytochrome c oxidase into electrode supported lipid bilayer at four crucial stages with molecular resolution. We were able to reveal the formation of a densely packed monolayer of the active ester dithio(succiniimidylepropionate) (DTSP) and the covalent linkage of the nitrilotriacetic acid (NTA) to the thiol anchored DTSP by scanning tunneling microscopy. Atomic force microscopy investigations showed that the detergent solubilized oxidase is immobilized as monomers and small aggregates via histidine residues. Finally, the reconstitution of the proteins within the supported membrane was verified. The amount of oxidase immobilized within the solid supported membrane was estimated.
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000047540 650_2 $$2MeSH$$aElectrodes
000047540 650_2 $$2MeSH$$aElectron Transport Complex IV: chemistry
000047540 650_2 $$2MeSH$$aGold: chemistry
000047540 650_2 $$2MeSH$$aMembranes, Artificial
000047540 650_2 $$2MeSH$$aMicroscopy, Scanning Probe: methods
000047540 650_2 $$2MeSH$$aParticle Size
000047540 650_2 $$2MeSH$$aSensitivity and Specificity
000047540 650_2 $$2MeSH$$aSurface Properties
000047540 650_7 $$00$$2NLM Chemicals$$aMembranes, Artificial
000047540 650_7 $$07440-57-5$$2NLM Chemicals$$aGold
000047540 650_7 $$0EC 1.9.3.1$$2NLM Chemicals$$aElectron Transport Complex IV
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000047540 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b2$$uFZJ
000047540 7001_ $$0P:(DE-Juel1)128713$$aOffenhäusser, A.$$b3$$uFZJ
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000047540 8567_ $$uhttp://hdl.handle.net/2128/2123$$uhttp://dx.doi.org/10.1021/la051195x
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