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|Title:||Modified cytochrome c/H2O2 system: spectroscopic EPR investigation of the biocatalytic behaviour||Authors:||Busi, Elena
Howes, B. D.
VAZQUEZ DUHALT, R.
|Keywords:||Cytochrome c; EPR; Spin trapping; Hemoprotein,; Peroxidase activity||Issue Date:||2000||Project:||None||Journal:||JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC||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 toinvestigate ways of improving the performance of Cyt crH2O2 oxidation systems, site-directed mutagenesis, and chemicalmodifications on the hemoprotein surface with polyethylene 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 ofthe chemical modified Cyt c PEG-Cyt-Met. and Cyt c mutants.
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