Evolved CYP102A1 (P450BM3) variants oxidise a range of non-natural substrates and offer new selectivity options†
Abstract
The evolution of CYP102A1 variants with enhanced activity and altered specificity characteristics.
* Corresponding authors
a
Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, UK
E-mail:
luet.wong@chem.ox.ac.uk
Fax: +44 1865 272690
The evolution of CYP102A1 variants with enhanced activity and altered specificity characteristics.
C. J. C. Whitehouse, S. G. Bell, H. G. Tufton, R. J. P. Kenny, L. C. I. Ogilvie and L. Wong, Chem. Commun., 2008, 966 DOI: 10.1039/B718124H
To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.
If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.
If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.
Read more about how to correctly acknowledge RSC content.
Fetching data from CrossRef.
This may take some time to load.
Loading related content