Structural studies on the dodecameric vanadium bromoperoxidase from Corallina species

The vanadium bromoperoxidase enzymes (VBPO) are receiving considerable interest since they show increased stability over the more commonly used heme chloroperoxidase enzymes. The multisubunit vanadium enzymes described in this article are exceptionally stable and offer the potential to be exploited for industrial catalysts. The multisubunit enzyme from Corallina officinalis was first crystallised in Exeter in a cubic form with cell dimensions of over 300 A. This made the structural solution a difficult problem (FEBS Lett. 359 (1995) 244). The structure of this enzyme has now been solved in our laboratory after its crystallisation in another more favourable tetragonal crystal form grown from a high concentration of phosphate (Acta Crystallogr. D 54 (1998) 454; J. Mol. Biol. 299 (2000) 1035). Recombinant vanadium haloperoxidase has recently been studied from the related C. pilulifera species. This enzyme has been purified and crystallised in the presence of high concentrations of phosphate, in a trigonal space group P6(3). The structure has been solved by molecular replacement using the wild-type C. officinalis structure as a model with which the C. pilulifera VBPO shows over 90% sequence identity. (C) 2002 Elsevier Science B.V. All rights reserved.