UV/Visible study of the reaction of oxidoreductases and model compounds with H2O2

FERREIRA, MARÍA LUJÁN

MACROMOLECULAR BIOSCIENCE

WILEY-V C H VERLAG GMBH

Año: 2003 vol. 3 p. 179 - 188

1616-5187

Oxidative dehydrogenation/polymerization of aromatic compounds such as phenol or aniline and derivatives has been reported using a peroxidase-H2O2 system. In the search for alternatives for expensive peroxidase, it is important to provide similar advantages to those of HRP while decreasing the catalyst cost. Knowledge of the mechanism details is important for achieving this objective. UV/Visible studies are useful to study mechanistic details and electronic changes in the compounds. These data are reported for the reaction of Catalase from Aspergillus Niger (CAP), Peroxidase from Horseradish (HRPC), Hematin and 2,6-bis[1-2,6-diisopropylphenyliminoethyl]pyridine iron(II) chloride (FeB) with H2O2. Detailed spectral analysis reveals differences for Catalase, Peroxidase, and model compounds in the presence of H2O2. The possibility of hematin or FeB-H2O2 as models for the peroxidase-H2O2 reaction is discussed. The published mechanisms for the peroxidase-H2O2 and Catalase-H2O2 reactions are analyzed. The results are discussed taking into account theoretical studies on some key aspects of the mechanism.