Abstract
AbstractZinc is one of the most abundant metals in living organisms and is an essential co‐factor of many metabolic enzymes and transcription factors. In this review, based on a recent body of theoretical and experimental results, the physical bases are delineated for the following aspects of zinc binding and selectivity in proteins: (1) What is the most thermodynamically preferable coordination geometry of a bidentate ligand (such as carboxylate) or Zn in Zn‐binding sites? (2) What is the protonation state of the Cys side chain in Cys4 zinc‐finger cores? (3) How does a protein select Zn from the mixture of ions in the surrounding fluids? (4) What is the role of the second shell in metal binding and selectivity? The key results are summarized and the physical basis and/or implications of the findings are discussed.
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