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Thermostabilization of a Cytochrome P450 Peroxygenase
Author(s) -
Salazar Oriana,
Cirino Patrick C.,
Arnold Frances H.
Publication year - 2003
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.200300660
Subject(s) - hydroxylation , hemeprotein , heme , cytochrome p450 , protein engineering , chemistry , biocatalysis , cytochrome , cytochrome p450 reductase , biochemistry , wild type , directed evolution , cytochrome c , stereochemistry , enzyme , mutant , catalysis , coenzyme q – cytochrome c reductase , gene , mitochondrion , ionic liquid
Some like it hot : We previously described a laboratory‐evolved variant of the cytochrome P450 BM‐3 heme domain which functions as a peroxide‐driven hydroxylase (peroxygenase, see picture). This biocatalyst does not require additional proteins or NADPH to drive hydroxylation and is amenable to further improvements through protein engineering. Here we describe a thermostable variant whose half‐life at 57.5 °C is 50 times that of the F87A variant and 250 times that of the wildtype holoenzyme.