Random sequential adsorption

Stoichiometric and site characteristics of the binding of iron to human transferrin.

Transferrin, biochemistry, physiology and clinical significance

Vanadium is an essential element. It is found widely distributed in minor and trace amounts throughout the lithosphere and biosphere. Vanadium is present in all mammalian tissues at concentrations of about 10 µM or less. Numerous physiological effects of this element are known at both the organismic and cellular levels, and in some instances these effects can be explained in terms of its biochemistry. Vanadate(V) and/or vanadyl(IV) ions are very potent inhibitors (K1 ≲ 10−6 M) of certain phosphatases, ATPases, phosphotransferases, nucleases, and kinases, among others. Vanadate(V) activates adenylate kinase. These ions have been quite useful as kinetic and spectroscopic (EPR) probes of complex cellular processes. Vanadium is an insulin mimetic agent. The ability of vanadium at low concentrations to influence enzymes is probably important to its function in vivo. Much of the biochemistry of vanadium is intricately related to the redox and coordination chemistry of this element. In particular, the parallel between the chemistries of vanadates and phosphates can account for the observed inhibition of various phosphohydrolases. However, there is ample evidence that vanadium in the body exists primarily as the vanadyl(IV) ion, VO2+, complexed to proteins and other cellular components; several biological reducing agents can convert vanadium(V) to this form. Serum transferrin appears to be involved in the metabolism of vanadium, perhaps as the transport protein for VO2+. Despite recent major advances in our understanding of the biochemistry of vanadium, the delineation of the physiological function(s) of this important element has remained an elusive goal.

The biochemistry of vanadium

http://www.jbc.org/content/258/6/3543.full.pdf

The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure

Proteins of iron metabolism

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Proteins of iron metabolism