• Title of article

    Modified cytochrome c/H2O2 system: spectroscopic EPR investigation of the biocatalytic behaviour

  • Author/Authors

    Busi، نويسنده , , E and Howes، نويسنده , , B.D and Pogni، نويسنده , , R and Basosi، نويسنده , , R and Tinoco، نويسنده , , R and Vazquez-Duhalt، نويسنده , , R، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2000
  • Pages
    10
  • From page
    39
  • To page
    48
  • Abstract
    In recent years there has been growing interest in methods for the degradation of polycyclic aromatic hydrocarbons. Cytochrome c (Cyt c) systems in the presence of H2O2 are able to oxidize various aromatic compounds. In order to investigate ways of improving the performance of Cyt c/H2O2 oxidation systems, site-directed mutagenesis, and chemical modifications on the hemoprotein surface with poly(ethylene glycol) and methylation of the active site have been performed. The EPR technique and UV–VIS spectroscopy have been used to identify radical intermediates and heme iron spin states of the chemical modified Cyt c (PEG-Cyt-Met) and Cyt c mutants.
  • Keywords
    Spin trapping , hemoprotein , peroxidase activity , cytochrome c , EPR
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Serial Year
    2000
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Record number

    1708443