Experimental and Computational Study of the Group 1 Metal Cation Chelates with Lysine: Bond Dissociation Energies, Structures, and Structural Trends

The kinetic energy dependence of the collision-induced dissociation (CID) of Group 1 metal cations (M + = Li +, Na +, K +, Rb +, and Cs + ) chelated to the amino acid lysine (Lys) was measured by threshold CID using a guided ion beam tandem mass spectrometer. The simple loss of neutral lysine is the only dissociation channel observed with the heavier alkali metal cations, whereas CID of Li + (Lys) yields other competing channels including loss of NH 3 (the dominant channel at low energy) and eight other reactions. Analysis of the kinetic energy-dependent cross sections yields experimental M + (Lys) bond dissociation energies (BDEs) of 376 ± 30, 219 ± 13, 160 ± 10, 141 ± 6, and 128 ± 4 kJ/mol for Li +, Na +, K +, Rb +, and Cs +, respectively. Computational searches yielded 18 distinct, low-energy structural families related to sites of M + binding in M + (Lys) complexes and 10 distinct, low-energy structural families for neutral lysine. Among the four levels of theory and three basis sets used, four different ground conformers of M + (Lys) and four different ground conformers of lysine were found, including a ground conformer of K + (Lys) and Cs + (Lys), [N ε,CO(OH)], and its higher energy zwitterionic analogue, [N ε,CO 2 – ], that better explains recent infrared multiple photon dissociation action spectroscopy results. Computational results for predicted ground structures of M + (Lys) complexes yielded computed BDEs in reasonable agreement with experiment.