The enzyme, found in some amino acid-fermenting anaerobic bacteria, participates in the fermentation pathways of L-phenylalanine, L-tyrosine, and L-tryptophan. It is a heterodimeric protein consisting of the FldB and FldC polypeptides, both of which contain an [4Fe-4S] cluster, and forms a complex with EC 2.8.3.17, 3-(aryl)acryloyl-CoA:(R)-3-(aryl)lactate CoA-transferase (FldA). In order to catalyse the reaction, the enzyme requires one high-energy electron that transiently reduces the electrophilic thiol ester carbonyl of the substrate to a nucleophilic ketyl radical anion, facilitating the elimination of the hydroxyl group. This electron, which is provided by by EC 5.6.1.9, (R)-2-hydroxyacyl-CoA dehydratase activating ATPase, needs to be supplied only once, before the first reaction takes place, as it is regenerated at the end of each reaction cycle. The enzyme acts on (R)-3-(aryl)lactoyl-CoAs produced by FldA, and regenerates the CoA donors used by that enzyme.
