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 N Daff, Caroline S Miles, Stephen K Chapman, Dominikus A Lysek, Christopher C Moser, Christopher C Page, P Leslie Dutton

    Research output: Contribution to journalLiterature reviewpeer-review

    342 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 - May 2002

    Keywords

    • CATALYTIC CYCLE
    • P-450 BM3
    • DOMAIN MOVEMENT
    • BINDING
    • ELECTRON-TRANSFER
    • REDUCTASE
    • PROTEIN
    • CYTOCHROME P450
    • BACILLUS-MEGATERIUM
    • SUBSTRATE

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