Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/76722
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Type: Journal article
Title: Tailoring an alien ferredoxin to support native-like P450 monooxygenase activity
Author: Bell, S.
McMillan, J.
Yorke, J.
Kavanagh, E.
Johnson, E.
Wong, L.
Citation: Chemical Communications, 2012; 48(95):11692-11694
Publisher: Royal Soc Chemistry
Issue Date: 2012
ISSN: 1359-7345
1364-548X
Statement of
Responsibility: 
Stephen G. Bell, James H. C. McMillan, Jake A. Yorke, Emma Kavanagh, Eachan O. D. Johnson, and Luet-Lok Wong
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.
Keywords: Sulfur
Iron
Cytochrome P-450 Enzyme System
Ferredoxins
Recombinant Proteins
Protein Structure, Tertiary
Protein Binding
Electron Transport
Oxidation-Reduction
Kinetics
Mutation
Rights: © Royal Society of Chemistry 2012
DOI: 10.1039/c2cc35968e
Published version: http://dx.doi.org/10.1039/c2cc35968e
Appears in Collections:Aurora harvest 4
Chemistry publications

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