X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata

In order to investigate the dual function of the dehaloperoxidase from the terebellid polychaete Amphitrite ornata, the enzyme was expressed in Escherichia coli as a recombinant protein in its wild-type form and as a mutant protein. Both the wild-type and mutant proteins were crystallized and their structures were determined at 100 K to a resolution of 1.62 Å.