Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4473
Title: Modified cytochrome c/H2O2 system: spectroscopic EPR investigation of the biocatalytic behaviour
Authors: Busi, Elena 
Howes, B. D.
Pogni, Rebecca 
Basosi, Riccardo 
Tinoco, R.
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.
Description: 
35303
URI: http://hdl.handle.net/20.500.12779/4473
ISSN: 1381-1177
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