P450 BM3: The very model of a modern flavocytochrome

Andrew W. Munro, David G. Leys, Kirsty J. McLean, Ker R. Marshall, Tobias W.B. Ost, Simon Daff, Caroline S. Miles, Stephen K. Chapman, Dominikus A. Lysek, Christopher C. Moser, Christopher C. Page, P. Leslie Dutton

Research output: Contribution to journalReview articlepeer-review

351 Citations (Scopus)

Abstract

Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion arrangement affords it the highest catalytic activity of any P450 mono-oxygenase. This article discusses the fundamental properties of P450 BM3 and how progress with this model P450 has affected our comprehension of P450 systems in general.

Original languageEnglish
Pages (from-to)250-257
Number of pages8
JournalTrends in Biochemical Sciences
Volume27
Issue number5
DOIs
Publication statusPublished - 1 May 2002
Externally publishedYes

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