Electrostatic interactions, hydrogen bonding, and solvation effects can alter the free energies of ionizable functional groups in proteins and other enclosed porous architectures, allowing these nanostructures to tune acid-base chemistry as needed to support specific functions. Herein, we expand on this theme to examine how metal sites (M = H2, ZnII, CoII, CoI) affect the pKa of benzoic acid guests bound in discrete porphyrin nanoprisms (M3TriCage), which were chosen as model systems for better understanding how porous metalloporphyrin electrocatalysts might influence H+ transfer processes that are needed to support many important electrochemical reactions (e.g., reductions of H+, O2, or CO2). Lewis acidic CoII and ZnII ions increase the Brønsted acidities of the guests by 4 and 8 pKa units, respectively, while reduction of the CoII sites to anionic CoI sites produces an electrostatic potential that lowers acidity by ca. 4 units (8 units relative to the CoII state). Lacking functional metal sites, H6TriCage increases the acidity of the guests by just 2.5 pKa units despite the 12+ charge of the host and contributions from other factors (hydrogen bonding, pore hydration) that might stabilize the depro-tonated guests. Thus, the metal sites have dominant effects on acid-base chemistry in the M3TriCages, providing a larger pKa range (12.75 to ≥24.5 in CD3CN) for the encapsulated acid than attained via other confinement effects in proteins and artificial porous materials.
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Jones et al. (2024) studied this question.
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