Publication Details

Abstract

Reductive dehalogenases are a class of corrinoid and [4Fe-4S] clusterdependent enzymes that are arguably key to organohalide respiration. Recently, the first crystal structures for these enzymes were reported, including one representative of both a respiratory as well as a nonrespiratory catabolic reductive dehalogenase. The comparison made between both structures establishes two highly conserved elements: the configuration of the redox chain within the protein and the Tyr-Lys/Arg active site dyad involved in proton transfer to the substrate. In contrast, the substrate binding elements are highly distinct. These insights serve to guide further study of RdhA structure-function relationships.