Zinc is more widely used as a cofactor in proteins than any other transition metal ion. In addition to catalytic and structural functions, zinc(II) ions have a role in information transfer and cellular control. They bind transiently when proteins regulate zinc concentrations and re-distribute zinc and when proteins are regulated by zinc. Transient zinc-binding sites employ the same donors of amino acid side chains as catalytic and structural sites but differ in their coordination chemistry that can modulate zinc affinities over at least ten orders of magnitude. Redox activity of the cysteine ligands, multiple binding modes of the oxygen, sulfur and nitrogen donors, and protein conformational changes induce coordination dynamics in zinc sites and zinc ion mobility. Functional annotations of the remarkable variation of coordination environments in zinc proteomes need to consider how the primary coordination spheres interact with protein structure and dynamics, and the adaptation of coordination properties to the biological context in extracellular, cellular, or subcellular locations.
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