The heme monooxygenase cytochrome P450cam can be engineered to oxidize ethane to ethanol.

Journal article

(Graph Presented) 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 (CC 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. © 2005 Wiley-VCH Verlag GmbH and. Co. KGaA.

Authors: Xu, F; Bell, S; Lednik, J; Insley, A; Rao, Z

• Publication status: Published
• Journal: Angewandte Chemie (International ed. in English)
• Volume: 44
• Issue: 26
• Pages: 4029-4032
• Publication date: 2005-06-01
• DOI: 10.1002/anie.200462630
• EISSN: 1521-3773
• ISSN: 1433-7851
• Language: English
• Keywords: Camphor 5-Monooxygenase; Ethane; Oxidation-Reduction; Binding Sites; Mutation; Ethanol; Protein Engineering; Heme Oxygenase-1