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Over the past several decades, vanadium has increasingly attracted the interest of biologists and chemists. The discovery by Henze in 1911 that certain marine ascidians accumulate the metal in their blood cells in unusually large quantities has done much to stimulate research on the role of vanadium in biology. In the intervening years, a large number of studies have been carried out to investigate the toxicity of vanadium in higher animals and to determine whether it is an essential trace element. That vanadium is a required element for a few selected organisms is now well established. Whether vanadium is essential for humans remains unclear although evidence increasingly suggests that it probably is. The discovery by Cantley in 1977 that vanadate is a potent inhibitor of ATPases lead to numerous studies of the inhibitory and stimulatory effects of vanadium on phosphate metabolizing enzymes. As a consequence vanadates are now routinely used as probes to investigate the mechanisms of such enzymes. Our understanding of vanadium in these systems has been further enhanced by the work of Tracy and Gresser which has shown striking parallels between the chemistry of vanadates and phosphates and their biological compounds. The observation by Shechter and Karlish, and Dubyak and Kleinzeller in 1980 that vanadate is an insulin mimetic agent has opened a new area of research dealing with the hormonal effects of vanadium. The first vanadium containing enzyme, a bromoperoxidase from the marine alga Ascophyllum nodosum, was isolated in 1984 by Viltner.
"Volume 31, devoted solely to the role of vanadium in life processes, offers a comprehensive and timely account of this fascinating field by 37 distinguished, international authorities. Highlights the properties of the various oxidation states of vanadium, their affinity for biogenic ligands, the effects of vanadium species on enzyme activity, the role of vanadium in nitrogenases and haloperoxidases, and more."
The first comprehensive resource on the chemistry of vanadium, Vanadium: Chemistry, Biochemistry, Pharmacology, and Practical Applications has evolved from over a quarter century of research that concentrated on delineating the aqueous coordination reactions that characterize the vanadium(V) oxidation state. The authors distill information o
Vanadium is named after Vanadis, the most aristocratic of Norse goddesses, who symbolises beauty and fertility - essential features of vanadium chemistry. It is a ubiquitous trace element, with a surprising range of biological functions. In Bioinorganic Vanadium Chemistry, Dieter Rehder addresses the major aspects of vanadium chemistry related to living organisms and the mutual impact between biological and inorganic vanadium chemistry. Topics covered include: the history, natural occurrence, distribution and impact of vanadium inorganic aspects of the function of vanadium in biological systems interaction of aqueous vanadate and vanadyl with biogenic ligands vanadium coordination compounds the vanadium-carbon bond methods of characterisation of biogenic and model vanadium systems (EPR and ENDOR for oxovanadium(IV); 51V NMR for vanadium(V); XAS) vanadium in ascidians and polychaeta worms the concentration of vanadium in the form of amavadin by Amanita mushrooms vanadate-dependent haloperoxidases vanadium and the nitrogen cycle vanadate as energiser for bacteria, and vanadophores medicinal aspectsm including the anti-diabetic potential of vanadium compounds interaction of vanadium with proteins and protein substrates vanadium and phosphate-metabolising enzymes Bioinorganic Vanadium Chemistry conveys the essential aspects of vanadium bioinorganic chemistry, making this book a valuable complement to more general bioinorganic chemistry texts and more specialized topical reviews for researchers and students alike.
Vanadium has been reported to be an essential bio-element for certain organisms, including tunicates, bacteria and some fungi. This book aimed to describe the coordination chemistry of vanadium with biologically relevant ligands and presents synthesis of oxo, dioxo and oxoperoxovanadium(V) complexes. Most common oxidation states are +IV and +V and generally stabilized through V-O bond. Oxocations [VO]2+, [VO]3+ and [VO2]+ are most common for biological systems. The development of structural and functional model complexes of vanadium haloperoxidases is the key motive of vanadium chemistry and some of the complexes can be considered to be structural models of haloperoxidases. The model character also extends to functional similarities, in that they catalyse the oxidation, by oxidant, of sulfoxide, styrene, cyclohexene, phenol, trans-stilbene etc. Vanadium complexes have also been found to catalyze the oxidation and epoxidation of various organic substrates. Some of the complexes have also been tested for their antiamoebic activity.