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Abstract
Enzymatic metal-mediated hydrolysis of phosphate esters may proceed through either inner- or outer-sphere pathways. Theoretical and experimental consideration of this problem suggests that outer-sphere pathways should predominate for magnesium-promoted reactions, where hydrogen bonding to metal-bound waters is the dominant stabilizing interaction, Comparison of a variety of magnesium-dependent enzymes reflects a requirement for differentially hydrated metal cofactor, which can only be achieved by limiting the number of protein ligands to the metal. As a result, these enzymes have evolved distinct mechanisms for control of metal binding affinities ( K D), all of which lie in the range of ∼0.5 mM. This article describes and discusses these issues, which have not previously been considered in detail.
Published Version
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