The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase

Rajasekhar Neeli, Hazel M. Girvan, Andrew Lawrence, Martin J. Warren, David Leys, Nigel S. Scrutton, Andrew W. Munro

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

In the model P450 BM3 system, the P450 is fused to its diflavin reductase partner in a single polypeptide. BM3 dimerizes in solution, but the catalytic relevance of the phenomenon was hitherto unknown. We show that BM3 fatty acid hydroxylase specific activity decreases sharply at low enzyme concentrations, consistent with separation of active dimer into inactive monomer. Reductase-dependent specific activities are maintained or enhanced at low concentration, suggesting inter-flavin electron transfer is unaffected. Fatty acid oxidation is reconstituted by mixing inactive oxygenase (A264H) and FMN-depleted (G570D) mutants, demonstrating that inter-monomer (FMN 1-to-heme2) electron transfer supports oxygenase activity in the BM3 dimer.

Original languageEnglish
Pages (from-to)5582-5588
Number of pages7
JournalFEBS Letters
Volume579
Issue number25
Early online date28 Sep 2005
DOIs
Publication statusPublished - 24 Oct 2005
Externally publishedYes

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