Catalytic properties of natural and artificial dehaloperoxidases

Dehaloperoxidases (DHPs) from Amphitrite ornata are unique heme proteins that merge reversible O 2 binding with peroxide-driven oxidation chemistry within a globin fold. This review first summarizes key discoveries that have clarified the molecular basis of the functional switch between DHP's oxygen-transport and catalytic roles, highlighting the structural and dynamic features that enable the protein to accommodate these seemingly incompatible activities. We then discuss DHP's catalytic properties, focusing on how substrate identity dictates its catalytic fate and redirects the enzyme among peroxidase-, peroxygenase-, and oxidase-like reaction pathways. Particular emphasis is placed on how substrate binding, active-site dynamics, and the heme environment cooperate to modulate reactive intermediates and, consequently, the observed product outcome. Finally, we discuss artificial metalloenzymes inspired by DHP, highlighting how this enzyme's distinctive properties have guided the design of biocatalysts that reproduce or expand its oxidative repertoire.