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Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/76722
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dc.contributor.authorBell, S.-
dc.contributor.authorMcMillan, J.-
dc.contributor.authorYorke, J.-
dc.contributor.authorKavanagh, E.-
dc.contributor.authorJohnson, E.-
dc.contributor.authorWong, L.-
dc.date.issued2012-
dc.identifier.citationChemical Communications, 2012; 48(95):11692-11694-
dc.identifier.issn1359-7345-
dc.identifier.issn1364-548X-
dc.identifier.urihttp://hdl.handle.net/2440/76722-
dc.description.abstractA 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.-
dc.description.statementofresponsibilityStephen G. Bell, James H. C. McMillan, Jake A. Yorke, Emma Kavanagh, Eachan O. D. Johnson, and Luet-Lok Wong-
dc.language.isoen-
dc.publisherRoyal Soc Chemistry-
dc.rights© Royal Society of Chemistry 2012-
dc.source.urihttp://dx.doi.org/10.1039/c2cc35968e-
dc.subjectSulfur-
dc.subjectIron-
dc.subjectCytochrome P-450 Enzyme System-
dc.subjectFerredoxins-
dc.subjectRecombinant Proteins-
dc.subjectProtein Structure, Tertiary-
dc.subjectProtein Binding-
dc.subjectElectron Transport-
dc.subjectOxidation-Reduction-
dc.subjectKinetics-
dc.subjectMutation-
dc.titleTailoring an alien ferredoxin to support native-like P450 monooxygenase activity-
dc.typeJournal article-
dc.identifier.doi10.1039/c2cc35968e-
pubs.publication-statusPublished-
dc.identifier.orcidBell, S. [0000-0002-7457-9727]-
Appears in Collections:Aurora harvest 4
Chemistry publications

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