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https://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 |
DOI: | 10.1039/B718124H |
Published version: | http://dx.doi.org/10.1039/b718124h |
Appears in Collections: | Aurora harvest Chemistry and Physics publications |
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