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@ARTICLE{Nyquist:32452,
      author       = {Nyquist, R. and Heitbrink, D. and Bolwien, C. and Wells, T.
                      A. and Gennis, R. B. and Heberle, J.},
      title        = {{D}irect {O}bservation of {P}rotonation {R}eactions during
                      the {C}atalytic {C}ycle of {C}ytochrome c {O}xidase},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {100},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PreJuSER-32452},
      pages        = {8715 - 8720},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Cytochrome c oxidase, the terminal protein in the
                      respiratory chain, converts oxygen into water and helps
                      generate the electrochemical gradient used in the synthesis
                      of ATP. The catalytic action of cytochrome c oxidase
                      involves electron transfer, proton transfer, and O2
                      reduction. These events trigger specific molecular changes
                      at the active site, which, in turn, influence changes
                      throughout the protein, including alterations of amino acid
                      side chain orientations, hydrogen bond patterns, and
                      protonation states. We have used IR difference spectroscopy
                      to investigate such modulations for the functional
                      intermediate states E, R2,Pm, and F. These spectra reveal
                      deprotonation of its key glutamic acid E286 in the E and in
                      the Pm states. The consecutive deprotonation and
                      reprotonation of E286 twice within one catalytic turnover
                      illustrates the role of this residue as a proton shuttle. In
                      addition, the spectra point toward deprotonation of a
                      redox-active tyrosine, plausibly Y288, in the F
                      intermediate. Structural insights into the molecular
                      mechanism of catalysis based on the subtle molecular changes
                      observed with IR difference spectroscopy are discussed.},
      keywords     = {Biophysical Phenomena / Biophysics / Carbon Monoxide:
                      chemistry / Catalysis / Electron Transport / Electron
                      Transport Complex IV: chemistry / Electron Transport Complex
                      IV: genetics / Electron Transport Complex IV: metabolism /
                      Glutamic Acid: chemistry / Models, Molecular / Mutagenesis,
                      Site-Directed / Oxidation-Reduction / Protein Conformation /
                      Protons / Rhodobacter sphaeroides: enzymology / Rhodobacter
                      sphaeroides: genetics / Spectrophotometry, Infrared /
                      Protons (NLM Chemicals) / Glutamic Acid (NLM Chemicals) /
                      Carbon Monoxide (NLM Chemicals) / Electron Transport Complex
                      IV (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {000},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:12851460},
      pmc          = {pmc:PMC166378},
      UT           = {WOS:000184371000024},
      doi          = {10.1073/pnas.1530408100},
      url          = {https://juser.fz-juelich.de/record/32452},
}