The oxidation of phenolic compounds catalysed by cytochrome C peroxidase. Comparison with other peroxidases
Articolo
Data di Pubblicazione:
1996
Citazione:
The oxidation of phenolic compounds catalysed by cytochrome C
peroxidase. Comparison with other peroxidases / L. Casella, E. Monzani, M. Gullotti, E. Santelli, S. Poli, T. Beringhelli. - In: GAZZETTA CHIMICA ITALIANA. - ISSN 0016-5603. - 126:2(1996), pp. 121-125.
Abstract:
The catalytic oxidations of a series of para-substituted phenolic
compounds by cytochrome c peroxidase and hydrogen peroxide have been
investigated. In the oxidation of these substrates the enzyme exhibits
very low catalytic efficiency and little selectivity, compared to
horseradish peroxidase and chloroperoxidase. The main reason for such a
low activity seems the limited size of the access channel leading from
the outside of the protein to the haem delta-meso edge, where the
substrate binding and electron transfer to the haem apparently occur.
Support to this view comes from preliminary relaxation rate
measurements. These show that the phenolic substrates can actually
approach the iron site but the nonlinearity of the relaxation rate vs.
enzyme bound fraction plots is indicative of a process limited by
chemical exchange.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
L. Casella, E. Monzani, M. Gullotti, E. Santelli, S. Poli, T. Beringhelli
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