Page 2 of 33 A c c e p t e d M a n u s c r i p t Novel Class III peroxidase biocatalyst from Chamaerops excelsa palm tree. The steady state kinetic mechanism of the H 2 O 2-supported oxidation of different organic substrates by this peroxidase (CEP) has been proposed. An analysis of the initial rates versus H 2 O 2 and reducing substrate concentrations is consistent with a substrate-inhibited Bi-Bi Ping-Pong reaction mechanism.
Plant peroxidases are presently used extensively in a wide range of biotechnological applications owing to their high environmental and thermal stability. As part of efforts towards the discovery of appealing new biotechnological enzymes, the peroxidase from leaves of the palm tree Chamaerops excelsa (CEP) was extracted, purified and crystallized in its native form. An X-ray diffraction data set was collected at a synchrotron source and data analysis showed that the CEP crystals belonged to the orthorhombic space group P2 1 2 1 2 1 , with unit-cell parameters a = 70.2, b = 100.7, c = 132.3 Å .
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