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 journalArticlepeer-review

    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 pages7
    JournalTrends in Biochemical Sciences
    Volume27
    Issue number5
    DOIs
    Publication statusPublished - 1 May 2002

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