title: The role of vanadium in biology.
abstract: Vanadium is special in at least two respects: on the one hand, the tetrahedral anion vanadate(v) is similar to the phosphate anion; vanadate can thus interact with various physiological substrates that are otherwise functionalized by phosphate. On the other hand, the transition metal vanadium can easily expand its sphere beyond tetrahedral coordination, and switch between the oxidation states +v, +iv and +iii in a physiological environment. The similarity between vanadate and phosphate may account for the antidiabetic potential of vanadium compounds with carrier ligands such as maltolate and picolinate, and also for vanadium's mediation in cardiovascular and neuronal defects. Other potential medicinal applications of more complex vanadium coordination compounds, for example in the treatment of parasitic tropical diseases, may also be rooted in the specific properties of the ligand sphere. The ease of the change in the oxidation state of vanadium is employed by prokarya (bacteria and cyanobacteria) as well as by eukarya (algae and fungi) in respiratory and enzymatic functions. Macroalgae (seaweeds), fungi, lichens and Streptomyces bacteria have available haloperoxidases, and hence enzymes that enable the 2-electron oxidation of halide X(-) with peroxide, catalyzed by a Lewis-acidic V(V) center. The X(+) species thus formed can be employed to oxidatively halogenate organic substrates, a fact with implications also for the chemical processes in the atmosphere. Vanadium-dependent nitrogenases in bacteria (Azotobacter) and cyanobacteria (Anabaena) convert N2 + H(+) to NH4(+) + H2, but are also receptive for alternative substrates such as CO and C2H2. Among the enigmas to be solved with respect to the utilization of vanadium in nature is the accumulation of V(III) by some sea squirts and fan worms, as well as the purport of the nonoxido V(IV) compound amavadin in the fly agaric.
authors.affiliation: Chemistry Department, University of Hamburg, 20146 Hamburg, Germany. rehder@chemie.uni-hamburg.de.
authors.forename: Dieter
authors.initials: D
authors.lastname: Rehder
mesh_terms: D000818:Animals; D001419:Bacteria / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism; D055808:Drug Discovery; D006801:Humans; D008958:Models, Molecular; D009591:Nitrogenase / Q000737:chemistry / Q000378:metabolism; D009195:Peroxidase / Q000737:chemistry / Q000378:metabolism; D014639:Vanadium / Q000032:analysis / Q000378:metabolism* / Q000494:pharmacology; D017968:Vanadium Compounds / Q000032:analysis / Q000378:metabolism* / Q000494:pharmacology
chemical_list: D017968:Vanadium Compounds; D014639:Vanadium; D009195:Peroxidase; D009591:Nitrogenase