Protein recognition of ammonium cations using side‐chain aromatics: A structural variation for secondary ammonium ligands

Abstract
A model for the structure of dimethylamine dehydrogenase was generated using the crystal coordinates of trimethylamine dehydrogenase. Substrate is bound in trimethylamine dehydrogenase by cation‐7r bonding, but modeling of dimethylamine dehydrogenase suggests that secondary amines are bound by a mixture of cation‐7r and conventional hydrogen bonding. In dimethylamine dehydrogenase, binding is orientationally more specific and distinct from those proteins that bind tertiary and quaternary amine groups.