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FEBS Lett. 1992 May 4;302(1):11-4.

(Model) studies on vanadate-dependent bromo/iodoperoxidase from Ascophyllum nodosum. VO2+ is not incorporated into the active site.

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Faculty of Inorganic Chemistry, University of Bielefeld, Germany.


Vanadate-dependent peroxidase A.n.I, the main isoenzyme (M(r) = 100 kDa) from the seaweed, Ascophyllum nodosum, contains 2 V per enzyme molecule (as shown by ICP-MS metal analysis) after complete reconstitution with vanadate (V), possibly distributed in a 1:1 ratio between the surface and active site. VO2+ is only weakly associated to the surface of A.n.I. There is no transport channel for VO2+. The EPR spectrum of the reduced holoenzyme is anisotropic (axial) already at room temperature, with EPR parameters similar to those of VO2+ complexes of small model peptides such as Ala-His, Gly-Tyr, Gly-Ser, Gly-Glu, Ser-Gly and Phe-Glu. The complex formation between Ala-His and H2VO4- in water has also been investigated (by 51V NMR); the formation constant at pH 7.2 amounts to 266(28) M-1.

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