Dehaloperoxidase: An enzymatic Swiss army knife

The hemoglobin from the marine worm Amphitrite ornata has been found to possess multiple enzymatic activities in addition to its O-2-transport function. Named dehaloperoxidase (DHP), this globin employs four mechanisms for substrate oxidation as a defense mechanism against toxic metabolites, spanning electron- (peroxidase and oxidase) and O-atom (peroxygenase and oxygenase) transfer. As such, DHP can be defined as a multifunctional catalytic hemoglobin. Given that its peroxidase function is already well established in the literature, this review aims to provide further structural and mechanistic details into the other three activities performed by DHP, with a particular emphasis on its peroxygenase activity. (C) 2021 Elsevier B.V. All rights reserved.