Vanadate activation of bromoperoxidase from Corallina officinalis.
A nonheme bromoperoxidase has been purified to homogeneity from the red seaweed Corallina officinalis. Like the corresponding enzyme previously reported from C. pilulifera, this bromoperoxidase contains a significant amount of nonheme iron. However, it is vanadate ion and not iron that activates the enzyme, and maximal activity is achieved with stoichiometric vanadium incorporation. The absence of competition between vanadium and iron suggests that they occupy distinct binding sites in the protein. A correlation between vanadium content and catalytic activity indicates that less than 12 percent of the maximal activity of the enzyme can be derived from metals other than vanadium.
Yu
H
H
Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
Whittaker
J W
JW
D001665:Binding Sites; D002384:Catalysis; D004578:Electron Spin Resonance Spectroscopy; D004789:Enzyme Activation / Q000187:drug effects; D007501:Iron / Q000378:metabolism; D008970:Molecular Weight; D010544:Peroxidases / Q000302:isolation & purification / Q000378:metabolism*; D012624:Seaweed / Q000201:enzymology*; D014638:Vanadates / Q000494:pharmacology*; D014639:Vanadium / Q000378:metabolism
D014639:Vanadium; D014638:Vanadates; D007501:Iron; D010544:Peroxidases; C026195:bromide peroxidase