Characterization of Cytochrome P450 Enzymes and Their Applications in Synthetic Biology

Laura N. Jeffreys, Hazel M. Girvan, Kirsty J. McLean, Andrew W. Munro

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

18 Citations (Scopus)


The cytochrome P450 monooxygenase enzymes (P450s) catalyze a diverse array of chemical transformations, most originating from the insertion of an oxygen atom into a substrate that binds close to the P450 heme. The oxygen is delivered by a highly reactive heme iron-oxo species (compound I) and, according to the chemical nature of the substrate and its position in the active site, the P450 can catalyze a wide range of reactions including, e.g., hydroxylation, reduction, decarboxylation, sulfoxidation, N- and O-demethylation, epoxidation, deamination, C–C bond formation and breakage, nitration, and dehalogenation. In this chapter, we describe the structural, biochemical, and catalytic properties of the P450s, along with spectroscopic and analytical methods used to characterize P450 enzymes and their redox partners. Important uses of P450 enzymes are highlighted, including how various P450s have been exploited for applications in synthetic biology.

Original languageEnglish
Title of host publicationEnzymes in Synthetic Biology
EditorsNigel Scrutton
PublisherAcademic Press Inc.
Number of pages73
ISBN (Print)9780128151488
Publication statusPublished - 1 Sep 2018
Externally publishedYes

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988


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