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@ARTICLE{Ataka:43304,
      author       = {Ataka, K. and Giess, F. and Knoll, W. and Naumann, R. and
                      Haber-Pohlmeier, S. and Richter, B. and Heberle, J.},
      title        = {{O}riented attachment and membrane reconstitution of
                      {H}is-tagged cytochrome c oxidase to a gold electrode:
                      in-situ monitoring by {S}urface {E}nhanced {I}nfrared
                      {A}bsorption {S}pectroscopy},
      journal      = {Journal of the American Chemical Society},
      volume       = {126},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-43304},
      pages        = {16199 - 16206},
      year         = {2004},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {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.},
      keywords     = {Electrochemistry / Electron Transport Complex IV: chemistry
                      / Enzymes, Immobilized: chemistry / Gold: chemistry /
                      Histidine: chemistry / Lipid Bilayers: chemistry / Models,
                      Molecular / Nitrilotriacetic Acid: chemistry / Recombinant
                      Proteins: chemistry / Spectroscopy, Fourier Transform
                      Infrared: methods / Surface Properties / Enzymes,
                      Immobilized (NLM Chemicals) / Lipid Bilayers (NLM Chemicals)
                      / Recombinant Proteins (NLM Chemicals) / Nitrilotriacetic
                      Acid (NLM Chemicals) / Histidine (NLM Chemicals) / Gold (NLM
                      Chemicals) / Electron Transport Complex IV (NLM Chemicals) /
                      J (WoSType)},
      cin          = {IBI-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Chemistry, Multidisciplinary},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15584756},
      UT           = {WOS:000225697000055},
      doi          = {10.1021/ja045951h},
      url          = {https://juser.fz-juelich.de/record/43304},
}