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@ARTICLE{Ataka:51339,
      author       = {Ataka, K. and Richter, B. and Heberle, J.},
      title        = {{O}rientational control on the physiological reaction of
                      cytochrome c oxidase tethered to a gold electrode},
      journal      = {The journal of physical chemistry / B},
      volume       = {110},
      issn         = {1520-6106},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PreJuSER-51339},
      pages        = {9339 - 9347},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The physiological reaction of a membrane protein is
                      reconstituted on a solid-supported electrode by
                      orientational control via the position of an affinity tag.
                      Recombinant cytochrome c oxidase (CcO) from Rhodobacter
                      sphaeroides is immobilized on a chemically modified gold
                      surface via the affinity of a histidine tag (His-tag) to a
                      nickel chelating nitrilotriacetic acid surface. Control of
                      the orientation is achieved by the adsorption of CcO through
                      the His-tag engineered into the two opposite sites of the
                      membrane protein surface. After reconstitution into a lipid
                      layer, the functionality of this enzyme film electrode is
                      probed by surface-enhanced infrared absorption spectroscopy
                      and cyclic voltammetry. We demonstrate that cytochrome c
                      (Cc) binds and initiates the catalytic reaction of CcO only
                      when the latter is orientated with subunit II facing the
                      bulk aqueous phase while Cc does not interact with the
                      oppositely orientated CcO. We infer from the observed
                      catalytic dioxygen reduction at potentials below 240 mV (vs
                      a normal hydrogen electrode) that reduced Cc mediates
                      electron input into CcO in a way similar to the
                      physiological pathway. The quantitative analysis of the IR
                      spectra indicates the presence of an inactive population of
                      Cc bound to CcO at equal amounts as the redox-active
                      population. This methodological approach demonstrates that
                      the orientation of the membrane protein can be controlled
                      depending on the position of the affinity tag. The approach
                      is considered to be of general applicability as the
                      introduction of affinity tags is routine in current
                      biochemistry.},
      keywords     = {Adsorption / Electrochemistry / Electrodes / Electron
                      Transport Complex IV: chemistry / Electron Transport Complex
                      IV: isolation $\&$ purification / Electron Transport Complex
                      IV: physiology / Enzymes, Immobilized: chemistry / Gold:
                      chemistry / Kinetics / Membranes, Artificial / Models,
                      Molecular / Recombinant Proteins: chemistry / Rhodobacter
                      sphaeroides: chemistry / Spectroscopy, Fourier Transform
                      Infrared / Surface Properties / Enzymes, Immobilized (NLM
                      Chemicals) / Membranes, Artificial (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals) / Gold (NLM Chemicals)
                      / Electron Transport Complex IV (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBI-2},
      ddc          = {530},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Chemistry, Physical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16671753},
      UT           = {WOS:000237451300063},
      doi          = {10.1021/jp0534131},
      url          = {https://juser.fz-juelich.de/record/51339},
}