Flavocytochrome P450 BM3 and the origin of CYP102 fusion species

H. M. Girvan, T. N. Waltham, R. Neeli, H. F. Collins, K. J. McLean, N. S. Scrutton, D. Leys, A. W. Munro

Research output: Contribution to journalConference article

28 Citations (Scopus)

Abstract

Flavocytochrome P450 (cytochrome P450) BM3 is an intensively studied model system within the P450 enzyme superfamily, and is a natural fusion of a P450 to its P450 reductase redox partner. The fusion arrangement enables efficient electron transfer within the enzyme and a catalytic efficiency that cannot be matched in P450 systems from higher organisms. P450 BM3's potential for industrially relevant chemical transformations is now recognized, and variants with biotechnological applications have been constructed. Simultaneously, structural and mechanistic studies continue to reveal the intricate mechanistic details of this enzyme, including its dimeric organization and the relevance of this quaternary structure to catalysis. Homologues of BM3 have been found in several bacteria and fungi, indicating important physiological functions in these microbes and enabling first insights into evolution of the enzyme family. This short paper deals with recent developments in our understanding of structure, function, evolution and biotechnological applications of this important P450 system.

Original languageEnglish
Pages (from-to)1173-1177
Number of pages5
JournalBiochemical Society Transactions
Volume34
Issue number6
DOIs
Publication statusPublished - 25 Oct 2006
Externally publishedYes
Event8th International Symposium on Cytochrome P450 Biodiversity and Biotechnology - Swansea Medical School, Swansea, United Kingdom
Duration: 23 Jul 200627 Jul 2006
Conference number: 8

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