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

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Erscheinungsjahr:
2009
Medientyp:
Text
Schlagworte:
  • Halogenation
  • Peroxidase
  • Natural products
  • Heme
  • Cytochrome P-450 Enzyme System
  • Hemoglobins
  • Vanadium
  • Functional haloperoxidase model
  • Peroxide chemistry
  • Oxidation catalysis
  • Haloperoxidase
  • Bromocyclization
  • Arene bromination
  • Bromohydrin
  • Halogenation
  • Peroxidase
  • Natural products
  • Heme
  • Cytochrome P-450 Enzyme System
  • Hemoglobins
Beschreibung:
  • 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. © 2009 IUPAC, Publication date (Web): 29 June 2009.
Lizenz:
  • info:eu-repo/semantics/closedAccess
Quellsystem:
Forschungsinformationssystem der UHH
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oai:www.edit.fis.uni-hamburg.de:publications/6513db18-ec1e-4566-9de7-589c9388988e