The Heme Monooxygenase Cytochrome P450cam Can Be Engineered to Oxidize Ethane to Ethanol

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 P450cam—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...

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Veröffentlicht in:	Angewandte Chemie International Edition 2005-06, Vol.44 (26), p.4029-4032
Hauptverfasser:	Xu, Feng, Bell, Stephen G., Lednik, Jaka, Insley, Andrew, Rao, Zihe, Wong, Luet-Lok
Format:	Artikel
Sprache:	eng
Schlagworte:	alkane oxidation Binding Sites Camphor 5-Monooxygenase - chemistry Camphor 5-Monooxygenase - genetics Ethane - chemistry Ethanol - chemistry Heme Oxygenase-1 - chemistry heme proteins iron metalloenzymes Mutation Oxidation-Reduction protein engineering Protein Engineering - methods
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Beschreibung
Zusammenfassung:	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 P450cam—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.
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.200462630