Structural Aspects of Metal Liganding to Functional Groups in Proteins

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Metal ions serve a variety of functions in proteins. The most important function is to enhance the structural stability of the protein in the conformation required for biological function and to take part in the catalytic processes of enzymes. Metal ions can take part in trigger and control mechanisms by specifically altering or stabilizing a macromolecular conformation on binding. This chapter discusses the properties of metals that are useful in the structure and function of proteins, particularly enzymes, and the geometry of interaction of metals with the various chemical groups of proteins are emphasized. Ligands donate an electron pair to the bond and are generally negatively charged or neutral. Important in a study of metal-ligand interactions are the polarizability of both the metal ion and the ligand, the number of the ligands around each metal ion, and the stereochemistry of the resulting arrangement. The stereochemistry of liganding of metal ions in proteins is known for several proteins. Some selected examples follow with data derived from the Protein Data Bank are emphasized in the chapter. The metals in protein crystal structures discussed are— namely, (1) copper, (2) iron, (3) manganese, (4) zinc, (5) magnesium, and (6) calcium. In the cases in which two different metals are bound, information can be obtained on preferential sites for each metal in the presence of the other.

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