Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/75770
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Type: Journal article
Title: Evolved CYP102A1 (P450BM3) variants oxidise a range of non-natural substrates and offer new selectivity options
Author: Whitehouse, C.
Bell, S.
Tufton, H.
Kenny, R.
Ogilvie, L.
Wong, L.
Citation: Chemical Communications, 2008; 28(8):966-968
Publisher: Royal Soc Chemistry
Issue Date: 2008
ISSN: 1359-7345
1364-548X
Statement of
Responsibility: 
Christopher J. C. Whitehouse, Stephen G. Bell, Henry G. Tufton, Richard J. P. Kenny, Lydia C. I. Ogilvie and Luet-Lok Wong
Abstract: The evolution of CYP102A1 variants with enhanced activity and altered specificity characteristics.
Keywords: Bacillus megaterium; Benzene Derivatives; Naphthalenes; Cytochrome P-450 Enzyme System; NADPH-Ferrihemoprotein Reductase; Mixed Function Oxygenases; Bacterial Proteins; Directed Molecular Evolution; Mutagenesis; Enzyme Activation; Molecular Structure; Substrate Specificity; Oxidation-Reduction; Time Factors
Rights: © The Royal Society of Chemistry 2008
RMID: 0020121298
DOI: 10.1039/B718124H
Appears in Collections:Chemistry and Physics publications

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