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The Heme Monooxygenase Cytochrome P450 cam Can Be Engineered to Oxidize Ethane to Ethanol
Author(s) -
Xu Feng,
Bell Stephen G.,
Lednik Jaka,
Insley Andrew,
Rao Zihe,
Wong LuetLok
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200462630
Subject(s) - monooxygenase , chemistry , heme , cytochrome p450 , ethanol , substrate (aquarium) , cytochrome , hemeprotein , mutant , enzyme , biochemistry , stereochemistry , biology , gene , ecology
A NADH turnover rate of 741 min −1 in the oxidition of ethane to ethanol is observed with an engineered form of the heme monooxygenase cytochrome P450 cam —the first example of such activity for a P450 enzyme (GC analysis shown). Ethanol is formed at 78 min −1 (10.5 % coupling). The mutant is ≈45 % high‐spin in the absence of substrate, making it a useful platform for P450 structure–function studies.
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