Yu H, Whittaker J W
Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
Biochem Biophys Res Commun. 1989 Apr 14;160(1):87-92. doi: 10.1016/0006-291x(89)91624-0.
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.
一种非血红素溴过氧化物酶已从红藻珊瑚藻中纯化至同质。与先前报道的来自小球藻的相应酶一样，这种溴过氧化物酶含有大量的非血红素铁。然而，激活该酶的是钒离子而非铁，并且在化学计量的钒掺入时达到最大活性。钒和铁之间不存在竞争表明它们在蛋白质中占据不同的结合位点。钒含量与催化活性之间的相关性表明，该酶最大活性的不到12%可源自钒以外的金属。
