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000057463 0247_ $$2pmid$$apmid:16518850
000057463 0247_ $$2DOI$$a10.1002/bip.20501
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000057463 084__ $$2WoS$$aBiochemistry & Molecular Biology
000057463 084__ $$2WoS$$aBiophysics
000057463 1001_ $$0P:(DE-Juel1)VDB5396$$aAtaka, K.$$b0$$uFZJ
000057463 245__ $$aUse of Surface Enhanced Infrared Absorption Spectroscopy (SEIRA) to probe the functionality of a protein monolayer
000057463 260__ $$aNew York, NY$$bWiley$$c2006
000057463 300__ $$a415 - 419
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000057463 440_0 $$011661$$aBiopolymers$$v82$$x0006-3525$$y4
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000057463 520__ $$aWe present a novel infrared method to investigate the functionality of a protein monolayer tethered to a metal substrate. The approach employs Surface Enhanced Infrared Absorption Spectroscopy (SEIRAS), which renders high surface sensitivity by enhancing the signal of the adsorbed protein by up to approximately 2 orders of magnitude. We demonstrate that the electrochemically induced absorption changes of a cytochrome c monolayer can be observed with excellent signal-to-noise ratio when the protein is adhered to a modified gold surface. To probe membrane proteins, a concept is introduced for the oriented incorporation into solid supported lipid bilayers. Recombinant cytochrome c oxidase solubilized in detergent is immobilized on a chemically modified gold surface via the affinity of its histidine (His)-tag to a nickel-chelating nitro-triacetic acid (NTA) surface. The protein monolayer is reconstituted into the lipid environment by detergent removal. Changing the orientation of the protein with respect to the metal surface is achieved by inserting the His-tag on either side of the membrane protein surface. Orientational control is mandatory for experiments in which electrons are injected from the electrode into the protein. The presented methodology opens new avenues to study the mechanism of the biomedically relevant class of electron and voltage-gated proteins on the atomic level.
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000057463 650_2 $$2MeSH$$aElectrochemistry: instrumentation
000057463 650_2 $$2MeSH$$aElectrochemistry: methods
000057463 650_2 $$2MeSH$$aElectrodes
000057463 650_2 $$2MeSH$$aElectron Transport Complex IV: chemistry
000057463 650_2 $$2MeSH$$aElectron Transport Complex IV: metabolism
000057463 650_2 $$2MeSH$$aGold: chemistry
000057463 650_2 $$2MeSH$$aMembrane Proteins: chemistry
000057463 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000057463 650_2 $$2MeSH$$aModels, Molecular
000057463 650_2 $$2MeSH$$aProteins: chemistry
000057463 650_2 $$2MeSH$$aProteins: metabolism
000057463 650_2 $$2MeSH$$aSpectrophotometry, Infrared: instrumentation
000057463 650_2 $$2MeSH$$aSpectrophotometry, Infrared: methods
000057463 650_2 $$2MeSH$$aSurface Properties
000057463 650_2 $$2MeSH$$aTime Factors
000057463 650_7 $$00$$2NLM Chemicals$$aMembrane Proteins
000057463 650_7 $$00$$2NLM Chemicals$$aProteins
000057463 650_7 $$07440-57-5$$2NLM Chemicals$$aGold
000057463 650_7 $$0EC 1.9.3.1$$2NLM Chemicals$$aElectron Transport Complex IV
000057463 650_7 $$2WoSType$$aJ
000057463 65320 $$2Author$$amembrane protein
000057463 65320 $$2Author$$asurface tether
000057463 65320 $$2Author$$abioelectrochemistry
000057463 65320 $$2Author$$acytochrome c oxidase
000057463 65320 $$2Author$$aproton transfer
000057463 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b1$$uFZJ
000057463 773__ $$0PERI:(DE-600)1480801-8$$0PERI:(DE-600)1480801-8$$a10.1002/bip.20501$$gVol. 82, p. 415 - 419$$p415 - 419$$q82<415 - 419$$tBiopolymers$$v82$$x0006-3525$$y2006
000057463 8567_ $$uhttp://dx.doi.org/10.1002/bip.20501
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