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

Stephen G Bell; James H C McMillan; Jake A Yorke; Emma Kavanagh; Eachan O D Johnson; Luet-Lok Wong

doi:10.1039/c2cc35968e

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

Chem Commun (Camb). 2012 Dec 11;48(95):11692-4. doi: 10.1039/c2cc35968e.

Authors

Stephen G Bell¹, James H C McMillan, Jake A Yorke, Emma Kavanagh, Eachan O D Johnson, Luet-Lok Wong

Affiliation

¹ The School of Chemistry and Physics, The University of Adelaide, SA, Australia. stephen.bell@adelaide.edu.au

PMID: 23104016
DOI: 10.1039/c2cc35968e

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cytochrome P-450 Enzyme System / metabolism*
Electron Transport
Ferredoxins / chemistry
Ferredoxins / genetics
Ferredoxins / metabolism*
Iron / chemistry
Kinetics
Mutation
Oxidation-Reduction
Protein Binding
Protein Structure, Tertiary
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / metabolism
Sulfur / chemistry

Substances

Ferredoxins
Recombinant Proteins
Sulfur
Cytochrome P-450 Enzyme System
Iron