Experimental charge density of an L-phenylalanine formic acid complex with a short hydrogen bond determined at 25 K

Abstract

The experimental charge density and related atomic and bond topological properties of an L-phenylalanine formic acid complex were derived from a high resolution X-ray data set (sin θ/λ = 1.18 Å^–1/d = 0.42 Å) measured at 25 K. The complex consists of a zwitterionic and a cationic phenylalanine molecule with formate as counterion. Special focus was directed on the density distribution in the region of a strong O—H ·· O hydrogen bond (O ·· O = 2.491(1) Å) which is formed between the two phenylalanine units. The obtained results are compared with the 15 previously derived experimental amino acid charge density data, with various theoretical calculations at experimental geometries and with the complete set of topological descriptors based on ab initio calculations of the neutral forms of all 20 amino acids published recently in the literature. A comparison of all available data in this biologically important class of compounds gives an impression about the significance of the quantitative results from experimental and theoretical charge density determinations.