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Binding and transport of nonferrous metals by serum transferrin

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Less Common Metals in Proteins and Nucleic Acid Probes

Part of the book series: Structure and Bonding ((STRUCTURE,volume 92))

Abstract

Transferrin is the serum iron transport protein in a wide variety of species. Its normal function is to transport iron through the blood between sites of uptake, utilization and storage. The protein consists of two distinct lobes, each of which contains a high affinity metal binding site. This review describes the thermodynamics of metal binding at these two sites, including the unique requirement of a synergistic carbonate anion for strong metal complexation. Normally the transferrin in serum is only partially saturated with iron, so that the protein provides a significant concentration of vacant binding sites which can sequester other metal ions that enter the blood. This review emphasizes metals for which transferrin appears to play a significant role in serum transport. There is strong evidence that transferrin is the primary serum transport agent for Mn3+, Hf4+, the group 13 metal ions Al3+, Ga3+, and In3+, and the tetravalent actinides Pu4+, Th4+, Np4+, and Pa4+. Transferrin appears to play a lesser role in the binding and transport of the trivalent actinides Cm3+ and Am3+, the oxocations VO2+, VO +2 , and UO 2+2 , and several of the lanthanides. There is also evidence that some of the metal-transferrin complexes are recognized and transported across cell membranes by the transferrin receptor.

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  1. Department of Chemistry, University of Missouri-St. Louis, 63121, St. Louis, MO

    Wesley R. Harris

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Harris, W.R. (1998). Binding and transport of nonferrous metals by serum transferrin. In: Less Common Metals in Proteins and Nucleic Acid Probes. Structure and Bonding, vol 92. Springer, Berlin, Heidelberg . https://doi.org/10.1007/BFb0081079

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