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. Copyright (C) 2000 Elsevier Science B.V. 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.

Busi, E., Howes, B.D., Pogni, R., Basosi, R., Tinoco, R., Vazquez Duhalt, R. (2000). Modified cytochrome c/H2O2 system: spectroscopic EPR investigation of the biocatalytic behaviour. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 9(1-3), 39-48 [10.1016/S1381-1177(99)00082-X].

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

Busi, Elena;Pogni, Rebecca;Basosi, Riccardo;
2000-01-01

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. Copyright (C) 2000 Elsevier Science B.V. 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.
2000
Busi, E., Howes, B.D., Pogni, R., Basosi, R., Tinoco, R., Vazquez Duhalt, R. (2000). Modified cytochrome c/H2O2 system: spectroscopic EPR investigation of the biocatalytic behaviour. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 9(1-3), 39-48 [10.1016/S1381-1177(99)00082-X].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/32248
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