Substrate specificity of the Chamaerops excelsa palm tree peroxidase. A steady-state kinetic study

The steady state kinetic mechanism of the H2O2-supported oxidation of different organic substrates by peroxidase from leaves of Chamaerops excelsa palm trees (CEP) has been investigated. An analysis of the initial rates vs. H2O2 and reducing substrate concentrations is consistent with a substrate-inhibited Ping-Pong Bi Bi reaction mechanism. The phenomenological approach expresses the peroxidase Ping-Pong mechanism in the form of the Michaelis–Menten equation and leads to an interpretation of the effects in terms of the kinetic parameters KmH2O2,KmAH2,kcat,KSIH2O2,KSIAH2 and of the microscopic rate constants k1 and k3 of the shared three-step catalytic cycle of peroxidases.

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► Novel Class III peroxidase biocatalyst from Chamaerops excelsa palm tree.
► The steady state kinetic mechanism of the H2O2-supported oxidation of different organic substrates by this peroxidase (CEP) has been proposed.
► An analysis of the initial rates versus H2O2 and reducing substrate concentrations is consistent with a substrate-inhibited Ping-Pong Bi Bi reaction mechanism.
► The corresponding kinetic parameters KmH2O2,KmAH2,kcat,KSIH2O2,KSIAH2 and the microscopic rate constants k1 and k3 of the shared three-step catalytic cycle of peroxidases have been determined.