Absolute affinities of alpha-amino acids for Cu+ in the gas phase. A theoretical study

Ab initio calculations have been carried out on the [glycine-Cu](+), [serine-Cu](+), and [cysteine-Cu](+) complexes. Investigation of several types of structures for each complex shows that the preferred binding site of Cu+ involves chelation between the carbonyl oxygen and the amino nitrogen. With glycine, this leads to a complexation energy (best estimate of D-0) of 64.3 kcal/mol. Additional chelation with the alcohol group of serine or the thiol group of cysteine leads to larger binding energies, with cysteine binding more strongly than serine, in good agreement with a recent experimental scale of relative Cu+ affinities of all alpha-amino acids present in natural peptides. Combining this scale to the accurate determination of the Cu+ affinity of glycine from the present work leads to absolute values of Cu+ affinities of all amino acids. Calculations were also carried out on the complexes of Cu+ with water, ammonia, formaldehyde, and hydrogen sulfide. The geometrical and electronic structures of these complexes are used to analyze the binding of Cu+ to amino acids.