Journal
FEBS LETTERS
Volume 579, Issue 25, Pages 5582-5588Publisher
WILEY
DOI: 10.1016/j.febslet.2005.09.023
Keywords
cytochrome p450; oxygenase; dimerization; electron transfer; fatty acids; enzymology
Ask authors/readers for more resources
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 (FMN1-to-heme(2)) electron transfer supports oxygenase activity in the BM3 dimer. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available