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

摘要

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 K(H2O2, m), K(AH2, m), k(cat), K(H2O2, SI), K(AH2, SI) and of the microscopic rate constants k1 and k3 of the shared three-step catalytic cycle of peroxidases.