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@ARTICLE{Pereira:51337,
      author       = {Pereira, M. M. and Sousa, F. L. and Teixeira, M. and
                      Nyquist, R. M. and Heberle, J.},
      title        = {{A} tyrosine residue deprotonates during oxygen reduction
                      by the caa3 reductase from {R}hodothermus marinus},
      journal      = {FEBS letters},
      volume       = {580},
      issn         = {0014-5793},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-51337},
      pages        = {1350 - 1354},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Heme-copper oxygen reductases catalyze proton translocation
                      across the cellular membrane; this takes place during the
                      reaction of oxygen to water. We demonstrate with attenuated
                      total reflection-Fourier transform infrared (ATR-FTIR)
                      difference spectroscopy that a tyrosine residue of the
                      oxygen reductase from the thermohalophilic Rhodothermus
                      marinus becomes deprotonated in the transition from the
                      oxidized state to the catalytic intermediate ferryl state
                      P(M). This tyrosine residue is most probably Y256, the helix
                      VI tyrosine residue proposed to substitute for the D-channel
                      glutamic acid that is absent in this enzyme. Comparison with
                      the mitochondrial like oxygen reductase from Rhodobacter
                      sphaeroides suggests that proton transfer from a
                      strategically situated donor to the active site is a crucial
                      step in the reaction mechanism of oxygen reductases.},
      keywords     = {Binding Sites / Catalysis / Cytochromes a3: metabolism /
                      Oxidation-Reduction / Oxidoreductases / Oxygen: metabolism /
                      Protons / Rhodobacter sphaeroides: enzymology /
                      Rhodothermus: enzymology / Rhodothermus: metabolism /
                      Spectroscopy, Fourier Transform Infrared / Tyrosine:
                      chemistry / Cytochromes a3 (NLM Chemicals) / Protons (NLM
                      Chemicals) / Tyrosine (NLM Chemicals) / Oxygen (NLM
                      Chemicals) / Oxidoreductases (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 / Cell
                      Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16466722},
      UT           = {WOS:000235597700024},
      doi          = {10.1016/j.febslet.2006.01.055},
      url          = {https://juser.fz-juelich.de/record/51337},
}