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Title: Horseradish peroxidase oxidizes 1,2,4,5-tetramethoxybenzene by a cation radical mechanism

Source: In: Lignin enzymic and microbial degradation: Symposium international; 1987 April 23-24; Paris. Paris: Institut National De La Recherche Agronomique; 1987: 75-79.

Author(s)Kersten, Ph.-J.; Kayanaraman, B.; Hammel, K.E.; Kirk, T.K.

Publication Year: 1987  View PDF »

Category: Conference Proceedings

Abstract: Recent studies show that ligninase oxidizes various non-phenolic substrates by one electron to give cation radical intermediates. To investigate the possibility that other peroxidases my have a similar mechanism, we tested various methoxybenzenes as substrates with horseradish peroxidase and H2O2. We found that 1,2,4,5-tetramethoxy-benzene is a good substrate. The corresponding cation radical intermediate was detected directly by ESR spectroscopy, and product analyses indicated that 2.5-dimethoxy-p-benzoquinone is a final product of the oxidation. Experiments with H218O showed that the quinone oxygens come from water. These results are discussed in relation to the oxidation potentials of peroxidases.

Keywords: horseradish, peroxidase, 1,2,4,5-tetramethoxybenzene

File size: 260 kb(s)

Date posted: 09/26/2011
Current FPL Scientists associated with this product (listed alphabetically)
Hammel, Kenneth E.
Research Chemist
Kersten, Philip J.
Research Microbiologist

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