Cytochrome P450s: creating novel ligand sets

Harriet E. Seward, Hazel M. Girvan, Andrew W. Munro

Research output: Contribution to journalReview articlepeer-review

2 Citations (Scopus)


Cytochromes P450 are a ubiquitous group of hemoproteins that perform vital cellular reactions in all lifeforms. Until recently, it was thought that P450s contained non-covalently bound heme. However, it was established that covalent linkage of the heme macrocycle occurs naturally in one major group of the P450 superfamily. The reaction involves heme linkage to a conserved amino acid and is autocatalytic, occurring as a consequence of P450 turnover. This finding presents opportunities to engineer biotechnologically important P450s to covalently link the heme, in order to stabilize cofactor binding and to enhance operational stability of these P450s. This opportunity has been taken in studies on two important bacterial P450s and has produced variants with intriguingly different properties. In this article we survey the developments in the field, the relationships with heme macrocycle ligations in other proteins and the important impact that recent studies of heme ligation have had on our general appreciation of P450 structure and mechanism.

Original languageEnglish
Pages (from-to)3419-3426
Number of pages8
JournalDalton Transactions
Issue number21
Early online date26 Sep 2005
Publication statusPublished - 7 Nov 2005
Externally publishedYes


Dive into the research topics of 'Cytochrome P450s: creating novel ligand sets'. Together they form a unique fingerprint.

Cite this