Abstract
Oxidative dehydrogenation/polymerization of aromatic compounds such as phenol or aniline and derivatives has been reported using a peroxidase‐H~2~O~2~ 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 H~2~O~2~. Detailed spectral analysis reveals differences for Catalase, Peroxidase, and model compounds in the presence of H~2~O~2~. The possibility of hematin or FeB‐H~2~O~2~ as models for the peroxidase‐H~2~O~2~ reaction is discussed. The published mechanisms for the peroxidase‐H~2~O~2~ and Catalase‐H~2~O~2~ reactions are analyzed. The results are discussed taking into account theoretical studies on some key aspects of the mechanism.
UV/Visible spectra of CAP (Catalase concentration 72.4 U/mL).
magnified imageUV/Visible spectra of CAP (Catalase concentration 72.4 U/mL).