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Issue 95, 2012
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Tailoring an alien ferredoxin to support native-like P450 monooxygenase activity

Stephen G. Bell,*ab  James H. C. McMillan,b  Jake A. Yorke,b  Emma Kavanagh,b  Eachan O. D. Johnsonb  and  Luet-Lok Wong*b 
Author affiliations

* Corresponding authors

a The School of Chemistry and Physics, The University of Adelaide, North Terrace, Adelaide, Australia
E-mail: stephen.bell@adelaide.edu.au
Fax: +61 8 8303 4380
Tel: +61 8 8313 4822

b Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, UK
E-mail: luet.wong@chem.ox.ac.uk
Fax: +44 (0)1865 272690
Tel: +44 (0)1865 272619

Abstract

A ferredoxin associated with biological Fe–S cluster assembly has been remodelled to transfer electrons to a P450 enzyme and support substrate oxidation at 80% of the physiological ferredoxin activity, opening up the possibility of tailoring ferredoxins to reconstitute the activity of P450 enzymes for which the electron transfer partner proteins are not known.

Graphical abstract: Tailoring an alien ferredoxin to support native-like P450 monooxygenase activity

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Publication details

The article was received on 17 Aug 2012, accepted on 11 Oct 2012 and first published on 15 Oct 2012


Article type: Communication
DOI: 10.1039/C2CC35968E
Citation: Chem. Commun., 2012,48, 11692-11694

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    Tailoring an alien ferredoxin to support native-like P450 monooxygenase activity

    S. G. Bell, J. H. C. McMillan, J. A. Yorke, E. Kavanagh, E. O. D. Johnson and L. Wong, Chem. Commun., 2012, 48, 11692
    DOI: 10.1039/C2CC35968E

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