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@ARTICLE{Heitbrink:58498,
      author       = {Heitbrink, D. and Sigurdson, H. and Bolwien, C. and
                      Brzezinski, P. and Heberle, J.},
      title        = {{T}ransient binding of {CO} to {C}u({B}) in cytochrome c
                      oxidase is dynamically linked to structural changes around a
                      carboxyl group : a time-resolved step-scan {F}ourier
                      transform infrared investigation},
      journal      = {Biophysical journal},
      volume       = {82},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-58498},
      pages        = {1 - 10},
      year         = {2002},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The redox-driven proton pump cytochrome c oxidase is that
                      enzymatic machinery of the respiratory chain that transfers
                      electrons from cytochrome c to molecular oxygen and thereby
                      splits molecular oxygen to form water. To investigate the
                      reaction mechanism of cytochrome c oxidase on the single
                      vibrational level, we used time-resolved step-scan Fourier
                      transform infrared spectroscopy and studied the dynamics of
                      the reduced enzyme after photodissociation of bound carbon
                      monoxide across the midinfrared range (2300-950 cm(-1)).
                      Difference spectra of the bovine complex were obtained at
                      -20degreesC with 5 mus time resolution. The data demonstrate
                      a dynamic link between the transient binding of CO to Cu-B
                      and changes in hydrogen bonding at the functionally
                      important residue E(I-286). Variation of the pH revealed
                      that the pK(a) of E(I-286) is >9.3 in the fully reduced
                      CO-bound oxidase. Difference spectra of cytochrome c oxidase
                      from beef heart are compared with those of the oxidase
                      isolated from Rhodobacter sphaeroides. The bacterial enzyme
                      does not show the environmental change in the vicinity of
                      E(I-286) upon CO dissociation. The characteristic band shape
                      appears, however, in redox-induced difference spectra of the
                      bacterial enzyme but is absent in redox-induced difference
                      spectra of mammalian enzyme. In conclusion, it is
                      demonstrated that the dynamics of a large protein complex
                      such as cytochrome c oxidase can be resolved on the single
                      vibrational level with microsecond Fourier transform
                      infrared spectroscopy. The applied methodology provides the
                      basis for future investigations of the physiological
                      reaction steps of this important enzyme.},
      keywords     = {J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000173250500001},
      url          = {https://juser.fz-juelich.de/record/58498},
}