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

• Published in: Pure and applied chemistry Vol. 81; no. 7; pp. 1251 - 1264
• Main Authors: Hartung, Jens, Dumont, Yvonne, Greb, Marco, Hach, Diana, Köhler, Franz, Schulz, Heiko, Časný, Marian, Rehder, Dieter, Vilter, Hans
• Format: Journal Article
• Language: English
• Published: Berlin De Gruyter 30-06-2009; Walter de Gruyter GmbH
• Subjects: Alcohols; arene bromination; Bromine; bromocyclization; bromohydrin; Buffers; Ethane; functional haloperoxidase model; haloperoxidase; Hydrogen peroxide; Mass balance; oxidation catalysis; Peroxidase; peroxide chemistry; Sulfonic acid; vanadium
• ISSN: 0033-4545; 1365-3075
• DOI: 10.1351/PAC-CON-08-09-01

Peroxidase (PO) activity of vanadate(V)-dependent bromoperoxidase (BPO) I (
) [V
PO(
I)] was retained with a half-life time of ~60 days, if stored in H
-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 H
, KBr, and V
PO(
I) in phosphate-buffered, CH
CN-diluted media.