Structural Characterization of [VO(salicylhydroximate)(CH30H)] 3: Applications to the Biological Chemistry of Vanadium(V)

The biological chemistry of vanadium has garnered increased attention due to the recent isolation of vanadium enzymes capable of nitrogenase [l] and bromoperoxidase [2,3] activities. The latter enzymes, isolated from marine algae, contain a mono-nuclear V(V) active site [4] that does not appear to require redox chemistry in the catalytic mechanism. It is well established that bacteria and algae often produce low molecular weight chelating agents (siderophores) which will sequester metal ions and facilitate the transport of these nutrients into the cell [5]. The two major classes of siderophores are based on catecholate and hydroxamate metal ligands [6]. Because vanadium bromoperoxidase is isolated from algae and bacteria, we felt that it would be interestin