Soybean peroxidase (SBP), an acidic peroxidase isolated from the seed coat, has been shown to be an effective catalyst for the oxidation of a variety of organic compounds. In the present study, we demonstrate that SBP can catalyze halogenation reactions. In the presence of H2O2, SBP catalyzed the oxidation of bromide and iodide but not chloride. Veratryl alcohol (3,4-dimethoxybenzyl alcohol) served as a useful substrate for SBP-catalyzed halogenations yielding the 6-bromo derivative. Halogenation of veratryl alcohol was optimal at pHs below 2.5 with rates of 2.4 mu m/min, achieving complete conversions of 150-mu m veratryl alcohol in 24 h, The enzyme showed essentially no brominating activity at pHs above 5.5, SBP-catalyzed bromination of veratryl alcohol proceeded with a maximum reaction velocity, V-max)(apparent), of 5.8 x 10(-1) mu m/min, a K-m of 78 mu m and a catalytic efficiency (k(cat)/K-m of 1.37 x 10(5) M/min at pH 4.0, assuming all of the enzyme＇s active sites participate in the reaction. SBP also catalyzed the bromination of several other organic substrates including pyrazole to produce a single product l-bromopyrazole, indole to yield both 5-bromoindole and 5-hydroxyindole, and the decarboxylative bromination of 3,4 dimethoxy-trans-cinnamic acid to trans-2-bromo-1-(3,4 dimethoxyphenyl)ethylene A catalytic mechanism for SBP-catalyzed bromination has been proposed based on experimental results in this and related studies. (C) 2000 Elsevier Science Inc. All rights reserved.