Evidence for Two Ferryl Species in Chioroperoxidase Compound II.

Using a combination of density functional calculations and Mössbauer spectroscopy, we have examined chloroperoxidase compound II (CPO-II). The Mössbauer spectrum of CPO-ll suggests the presence of two distinct ferryl species in an ~70:30 ratio. Density functional calculations and cryogenic reduction...

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Publicado en:Journal of the American Chemical Society Vol. 128; no. 18; pp. 6147 - 6154
Autores principales: Stone, Karl L., Hoffart, Lee M., Behan, Rachel K., Krebs, Carsten, Green, Michael T.
Formato: Artículo
Publicado: American Chemical Society 5/10/2006
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Acceso en línea:Ver este registro en EBSCOhost
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      pub: American Chemical Society
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        10.1021/ja057876w
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        atl: Evidence for Two Ferryl Species in Chioroperoxidase Compound II.
      aug:
        au:
          Stone, Karl L.
          Hoffart, Lee M.
          Behan, Rachel K.
          Krebs, Carsten
          Green, Michael T.
        affil:
          Contribution from the Department of Chemistry and Biochemistry, The Pennsylvania State University, University Park, Pennsylvania 16802
          Department of Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802
      su:
        Peroxidase
        Iron compounds
        Mössbauer spectroscopy
        Chlorine compounds
        Density functionals
        Hydrogen-ion concentration
      sug:
        subj:
          Peroxidase
          Iron compounds
          Mössbauer spectroscopy
          Chlorine compounds
          Density functionals
          Hydrogen-ion concentration
      ab: Using a combination of density functional calculations and Mössbauer spectroscopy, we have examined chloroperoxidase compound II (CPO-II). The Mössbauer spectrum of CPO-ll suggests the presence of two distinct ferryl species in an ~70:30 ratio. Density functional calculations and cryogenic reduction and annealing experiments allow us to assign the major species as an Fe(IV)OH intermediate. The Mössbauer parameters of the minor component are indicative of an authentic iron(IV)oxo species, but we have found the 70:30 ratio to be pH invariant. The unchanging ratio of component concentrations is in agreement with CPO-ll's visible absorption spectrum, which shows no change over the enzyme's range of pH stability.
      pubtype: Academic Journal
      doctype: Article
      src: R
    language: English
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