Bromoperoxidase from Ascophyllum nodosum: a novel class of enzymes containing vanadium as a prosthetic group?

E. de Boer, Y. van Kooyk, M. G.M. Tromp, H. Plat, R. Wever

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Reconstitution experiments showed that the transition metal vanadium is essential for enzymic activity of bromoperoxidase from the marine brown alga Ascophyllum nodosum. A linear relationship existed between brominating activity and the amount of vanadium incorporated in the enzyme. Maximal activity was found when the enzyme contained 5.1 nmol vanadium per mg bromoperoxidase. Based on gel-exclusion high-performance liquid chromatography, the molecular mass of bromoperoxidase was estimated as 90 000. Chemical analysis and electron paramagnetic resonance (EPR) demonstrated that bromoperoxidase contains vanadium (4.4 nmol per mg bromoperoxidase). This value corresponds to a ratio of 0.4 mol vanadium per mol bromoperoxidase. The EPR experiments suggest that in bromoperoxidase the vanadium ion is present in the 5 + redox state. These experiments demonstrate for the first time the existence of an enzyme containing vanadium at the active site.

Original languageEnglish
Pages (from-to)48-53
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number1
Publication statusPublished - 17 Jan 1986


  • (A. nodosum)
  • Bromoperoxidase
  • ESR
  • Halometabolite
  • Prosthetic group
  • Vanadium

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