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Abstract
The aqueous chemistry of vanadate (vanadium(V)) is very complex since many protonation equilibria and oligomerization equilibria are occurring simultaneously. Vanadate monomer (V1), dimer (V2), tetramer (V4) and pentamer (V5) are exchanging with each other on a millisecond time scale so that none of these species can be isolated for aqueous biological studies. Measuring the effects of each anion on an enzyme must be carried out in an equilibrium mixture containing the other vanadate oligomers. Defining conditions to measure the effects of oxovanadates is non-trivial, since vanadate interacts with buffers and other assay components. Information concerning the simple aqueous chemistry of vanadate with various ligands is thus necessary to ensure that the vanadate is free to interact with an enzyme or a protein. Experimental approaches, which take into account the aqueous chemistry of labile oxovanadates, to biological studies are described here. For this purpose, the interactions of oxovanadates with proteins and other protein-like ligands are considered briefly. The chemistry and approaches described here form the basis for an analysis of the interactions of vanadate oxoanions with proteins.
