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@ARTICLE{Hrabakova:51336,
      author       = {Hrabakova, J. and Ataka, K. and Heberle, J. and
                      Hildebrandt, P. and Murgida, D.},
      title        = {{L}ong distance electron transfer in cytochrome c oxidase
                      immobilised on electrodes. {A} surface enhanced resonance
                      {R}aman spectroscopic study},
      journal      = {Physical Chemistry Chemical Physics},
      volume       = {8},
      issn         = {1463-9076},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {PreJuSER-51336},
      pages        = {759 - 766},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Cytochrome c oxidase was tethered to a functionalised Ag
                      electrode via a histidine-tag on the C-terminus of subunit I
                      or II and embedded in a phospholipid bilayer. The uniformly
                      oriented membrane-bound proteins were studied by surface
                      enhanced resonance Raman spectroscopy (SERRS) that reveals
                      preservation of the native structures of the heme a and heme
                      a(3) sites. On the basis of time-dependent SERRS
                      measurements, the rate constant for the heterogeneous
                      electron transfer to heme a was determined to be 0.002 s(-1)
                      independent of the enzyme orientation and the overpotential.
                      Taking into account that the electrode-to-heme a distance is
                      larger than 50 A, these findings suggest an electron hopping
                      mechanism in which the Cu(A) center is not involved.
                      Electrochemical reduction is restricted to heme a whereas
                      electron transfer from heme a to heme a(3), which in
                      solution occurs on the nanosecond time scale, is drastically
                      slowed down. It may be that the network of cooperativities
                      that links intramolecular electron transfer and proton
                      translocation is perturbed in the immobilised enzyme,
                      possibly due to the effect of the interfacial electric
                      field.},
      keywords     = {Chemistry, Physical / Electrodes / Electron Transport
                      Complex IV: chemistry / Enzymes, Immobilized: chemistry /
                      Models, Chemical / Oxidation-Reduction / Physicochemical
                      Phenomena / Silver: chemistry / Spectrum Analysis, Raman:
                      methods / Surface Properties / Time Factors / Enzymes,
                      Immobilized (NLM Chemicals) / Silver (NLM Chemicals) /
                      Electron Transport Complex IV (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Chemistry, Physical / Physics, Atomic, Molecular $\&$
                      Chemical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16482317},
      UT           = {WOS:000235608500011},
      doi          = {10.1039/b513379n},
      url          = {https://juser.fz-juelich.de/record/51336},
}