These authors contributed equally to this work.
The Heme Monooxygenase Cytochrome P450cam Can Be Engineered to Oxidize Ethane to Ethanol†
Article first published online: 24 MAY 2005
Copyright © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 44, Issue 26, pages 4029–4032, June 27, 2005
How to Cite
Xu, F., Bell, S. G., Lednik, J., Insley, A., Rao, Z. and Wong, L.-L. (2005), The Heme Monooxygenase Cytochrome P450cam Can Be Engineered to Oxidize Ethane to Ethanol. Angew. Chem. Int. Ed., 44: 4029–4032. doi: 10.1002/anie.200462630
L.-L.W. acknowledges support from the Biotechnology and Biological Sciences Research Council (UK) (B10666) and the Higher Education Funding Council for England.
- Issue published online: 17 JUN 2005
- Article first published online: 24 MAY 2005
- Manuscript Revised: 17 MAR 2005
- Manuscript Received: 16 NOV 2004
- alkane oxidation;
- heme proteins;
- protein engineering
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.