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P450 BM3: the very model of a modern flavocytochrome |
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| Authors: | Munro Andrew W Leys David G McLean Kirsty J Marshall Ker R Ost Tobias W B Daff Simon Miles Caroline S Chapman Stephen K Lysek Dominikus A Moser Christopher C Page Christopher C Dutton P Leslie |
| Affiliation: | 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. |
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