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@ARTICLE{Ataka:57463,
      author       = {Ataka, K. and Heberle, J.},
      title        = {{U}se of {S}urface {E}nhanced {I}nfrared {A}bsorption
                      {S}pectroscopy ({SEIRA}) to probe the functionality of a
                      protein monolayer},
      journal      = {Biopolymers},
      volume       = {82},
      issn         = {0006-3525},
      address      = {New York, NY},
      publisher    = {Wiley},
      reportid     = {PreJuSER-57463},
      pages        = {415 - 419},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {We 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.},
      keywords     = {Electrochemistry: instrumentation / Electrochemistry:
                      methods / Electrodes / Electron Transport Complex IV:
                      chemistry / Electron Transport Complex IV: metabolism /
                      Gold: chemistry / Membrane Proteins: chemistry / Membrane
                      Proteins: metabolism / Models, Molecular / Proteins:
                      chemistry / Proteins: metabolism / Spectrophotometry,
                      Infrared: instrumentation / Spectrophotometry, Infrared:
                      methods / Surface Properties / Time Factors / Membrane
                      Proteins (NLM Chemicals) / Proteins (NLM Chemicals) / Gold
                      (NLM Chemicals) / Electron Transport Complex IV (NLM
                      Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16518850},
      UT           = {WOS:000238241900027},
      doi          = {10.1002/bip.20501},
      url          = {https://juser.fz-juelich.de/record/57463},
}