Tailoring an alien ferredoxin to support native-like P450 monooxygenase activity

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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.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.identifier.citationChemical Communications, 2012; 48(95):11692-11694
dc.identifier.doi10.1039/c2cc35968e
dc.identifier.issn1359-7345
dc.identifier.issn1364-548X
dc.identifier.orcidBell, S. [0000-0002-7457-9727]
dc.identifier.urihttp://hdl.handle.net/2440/76722
dc.language.isoen
dc.publisherRoyal Soc Chemistry
dc.rights© Royal Society of Chemistry 2012
dc.source.urihttps://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
pubs.publication-statusPublished

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