Bromoperoxidases from the brown alga Ascophyllum nodosum, abbreviated as VBrPO (AnI) and VBrPO (AnII), show 41% sequence homology and differ by a factor of two in the percentage of α-helical secondary structures. Protein monomers organize into homodimers for VBrPO (AnI) and hexamers for VBrPO (AnII). Bromoperoxidase II binds hydrogen peroxide and bromide by approximately one order of magnitude stronger than VBrPO (AnI ...