Emmanuelle Bouveret

This study identifies a molecular link between iron-sulfur cluster biogenesis and fatty acid synthesis in E. coli through the interaction of ACP and IscS.

This paper shows that 2,4-dienoyl-CoA reductase (FadH) is essential for E. coli to degrade unsaturated fatty acids in complex mixtures and that eukaryotic DECR enzymes can functionally replace FadH.

The paper investigates why iron-sulphur cluster enzymes are often inactive when heterologously expressed in E. coli and identifies strategies to improve their functionality.