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Characterization of the Peroxidase Activity of CYP119, a Thermostable P450 From Sulfolobus acidocaldarius
Author(s) -
Rabe Kersten S.,
Kiko Kathrin,
Niemeyer Christof M.
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700450
Subject(s) - sulfolobus acidocaldarius , sulfolobus solfataricus , sulfolobus , enzyme , biochemistry , peroxidase , biocatalysis , chemistry , stereochemistry , biology , archaea , gene , catalysis , reaction mechanism
We report the cloning, expression, and purification of CYP119, a thermostable enzyme previously thought to derive from Sulfolobus solfataricus . Sequence analysis suggested that, in contrast to the conclusions of earlier studies, the enzyme stems from the closely related Sulfolobus acidocaldarius , and we were indeed able to clone the gene from the genomic DNA of this organism. For the first time, we report here on the peroxidase activity of this enzyme and the optimization of the associated reaction parameters. The optimized reaction conditions were then applied to the biocatalytic epoxidation of styrene. The values obtained for k cat (78.2±20.6 min −1 ) and K M (9.2±4.3 m M ) indicated an approximately 100‐fold increased catalytic activity over previously reported results.