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Pure Appl. Chem., 2009, Vol. 81, No. 7, pp. 1251-1264

Published online 2009-06-29

On the reactivity of bromoperoxidase I (Ascophyllum nodosum) in buffered organic media: Formation of carbon bromine bonds

Jens Hartung1*, Yvonne Dumont1, Marco Greb2, Diana Hach1, Franz Köhler2, Heiko Schulz1, Marian Časný3, Dieter Rehder3 and Hans Vilter4

1 Fachbereich Chemie, Organische Chemie, Technische Universität Kaiserslautern, Erwin-Schrödinger-Straße, 67663 Kaiserslautern, Germany
2 Institut für Organische Chemie, Universität Würzburg, Am Hubland, 97074 Würzburg, Germany
3 Institut für Anorganische und Angewandte Chemie, Universität Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany
4 Zurmaiener Straße 16, D-54292 Trier, Germany

Abstract: Peroxidase (PO) activity of vanadate(V)-dependent bromoperoxidase (BPO) I (Ascophyllum nodosum) [VBrPO(AnI)] was retained with a half-life time of ~60 days, if stored in H2O2-incubated, morpholin-4-ethane sulfonic acid (MES)-buffered aqueous alcoholic solutions. These conditions were applied for converting bromide and, e.g., methyl pyrrole-2-carboxylate into bromopyrroles with an almost quantitative peroxide yield. δ,ε-unsaturated alcohols furnished β-bromohydrins and products of bromocyclization, i.e., tetrahydrofurans and tetrahydropyrans (70–84 % mass balance), if treated with H2O2, KBr, and VBrPO(AnI) in phosphate-buffered, CH3CN-diluted media.