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

Authors

  • Feng Xu,

    1. Laboratory of Structural Biology, School of Life Sciences and Engineering, Tsinghua University, Beijing 100084, China, Fax: (+86) 10-6277-3145
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    • These authors contributed equally to this work.

  • Stephen G. Bell Dr.,

    1. Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK, Fax: (+44) 1865-272690
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    • These authors contributed equally to this work.

  • Jaka Lednik,

    1. Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK, Fax: (+44) 1865-272690
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  • Andrew Insley,

    1. Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK, Fax: (+44) 1865-272690
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  • Zihe Rao Prof.,

    1. Laboratory of Structural Biology, School of Life Sciences and Engineering, Tsinghua University, Beijing 100084, China, Fax: (+86) 10-6277-3145
    2. Institute of Biophysics, 15 Datun Road, Chaoyang District, Beijing 100101, China, Fax: (+86) 10-6486-7566
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  • Luet-Lok Wong Dr.

    1. Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK, Fax: (+44) 1865-272690
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  • L.-L.W. acknowledges support from the Biotechnology and Biological Sciences Research Council (UK) (B10666) and the Higher Education Funding Council for England.

Abstract

original image

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.

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