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 review

    321 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

    Cite this

    Munro, A. W., Leys, D. G., McLean, K. J., Marshall, K. R., Ost, T. W. B., Daff, S. N., Miles, C. S., Chapman, S. K., Lysek, D. A., Moser, C. C., Page, C. C., & Dutton, P. L. (2002). P450 BM3: the very model of a modern flavocytochrome. Trends in Biochemical Sciences, 27(5), 250-257. https://doi.org/10.1016/S0968-0004(02)02086-8