title: Tailoring an alien ferredoxin to support native-like P450 monooxygenase activity.
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.
authors.affiliation: The School of Chemistry and Physics, The University of Adelaide, SA, Australia. stephen.bell@adelaide.edu.au
authors.forename: Stephen G
authors.initials: SG
authors.lastname: Bell
authors.forename: James H C
authors.initials: JH
authors.lastname: McMillan
authors.forename: Jake A
authors.initials: JA
authors.lastname: Yorke
authors.forename: Emma
authors.initials: E
authors.lastname: Kavanagh
authors.forename: Eachan O D
authors.initials: EO
authors.lastname: Johnson
authors.forename: Luet-Lok
authors.initials: LL
authors.lastname: Wong
mesh_terms: D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004579:Electron Transport; D005288:Ferredoxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007501:Iron / Q000737:chemistry; D007700:Kinetics; D009154:Mutation; D010084:Oxidation-Reduction; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013455:Sulfur / Q000737:chemistry
chemical_list: D005288:Ferredoxins; D011994:Recombinant Proteins; D013455:Sulfur; D003577:Cytochrome P-450 Enzyme System; D007501:Iron