vanadate activation of bromoperoxidase from corallina officinalis
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336 Abstracts
LO84 VANADATE ACTIVATION OF BROMOPEROXIDASE FROM Corallina officinalis. H. Yu and J.W. Whittaker, Dept. of Chemistry,
Carnegie Mellon University, 4400 Fifth Ave., Pittsburgh, PA 15213, USA A nonheme bromoperoxidase has been purified to homogeneity from
the red seaweed Corallina officinalis. This enzyme has similar kinetic parameters to the corresponding bromoperoxidase from C. pilulifera, and similarly contains a significant amount of nonheme iron. However,
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vanadate ion rather than iron activates the enzyme, and maximal acti- vity is achieved with stoichiometric vanadium incorporation. A cor- relation between vanadium content and catalytic activity indicates that vanadium is essential to the bromoperoxidase activity. EPR spectra characteristic of V(IV) are observed on reduction, suggesting that the V is bound in a higher oxidation state complex. This enzyme thus appears to be a member of the growing class of vanadium haloperoxidases.