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    Trends Biochem Sci. 2002 May;27(5):250-7.

    P450 BM3: the very model of a modern flavocytochrome.

    Munro AW, Leys DG, McLean KJ, Marshall KR, Ost TW, Daff S, Miles CS, Chapman SK, Lysek DA, Moser CC, Page CC, Dutton PL.

    Department Biochemistry, University of Leicester, The Adrian Building, University Road, Leicester LE1 7RH, UK. awm9@le.ac.uk

    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.

    PMID: 12076537 [PubMed - indexed for MEDLINE]

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