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
Link To Document :
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