Tungstate-exchanged layered double hydroxides (LDHs) and V-bromoperoxidase enzymes perform oxidative brominations in a highly similar way: first H2O2 binds on the metal to form a peroxometal complex; next the peroxometal oxidizes Br- to "Br+"; this electrophilic "Br+" halogenates an organic compound, or oxidizes a second H2O2 Molecule to form excited state singlet oxygen. Full evidence for this similarity is given, based on spectroscopic observation of peroxotungstate and O-1(2) and on identification of the organic bromination products. In comparison with the homogeneous oxometallates, or with heterogeneous Ti-catalysts, the bioinspired LDH-WO42- catalyst displays much higher rates of Br- oxidation; this rate enhancement is explained. The activity of LDH-WO42- can be enhanced by changing the elemental composition of the octahedral layer of the LDH structure. Since LDH-WO42- is stable toward leaching and high H2O2 concentrations, it is a practical catalyst for oxidative bromination. (C) 2003 Elsevier Science (USA). All rights reserved.