Computation of through-space NMR shielding effects in aromatic ring pi-stacked complexes

Aromatic compounds can form dimeric complexes in solution. Substituted aromatics tend to form parallel-stacked complexes, either aligned or offset. The HF-GIAO method in Gaussian 03 was employed to calculate the NMR isotropic shielding values of the proximal hydrogen of diatomic hydrogen probes above and below the center of the ring and above and below an unsubstituted ring carbon of 1,3,5-trimethylbenzene in a face-to-face pi-stacked aligned complex with 1,3,5-trinitrobenzene. The calculated isotropic shielding values for the aromatic hydrogens of each of the substituted rings were subtracted from the isotropic shielding values calculated for the comparable positions in the complex. Complexation results in each aromatic ring shielding the other ring. Also, the calculated isotropic shielding values for the proximal hydrogen of a diatomic hydrogen probe over (or under) each of the individual substituted benzenes were subtracted from the isotropic shielding values calculated for the comparable positions in the complex. The difference is the shielding increment due to complexation. Complexation results in increased NMR shielding of a hydrogen probe molecule on both sides of the pi-stacked complex, with slightly more shielding due to complexation on the side nearest 1,3,5-trimethylbenzene. The results are interpreted in terms of polarization of the pi cloud of the substituted benzenes by complexation and its NMR consequences. Finally, NMR shielding calculations were done on the optimized structure of N-phenylpyrrole dimer. The data were compared to concentration-dependent NMR shift data to estimate the percent dimer present.     

Computation of through-space NMR shielding effects by small-ring aromatic and antiaromatic hydrocarbons

The GIAO-HF method in Gaussian 03 was employed to calculate the isotropic NMR shielding values of a diatomic hydrogen probe above simple small-ring aromatic and antiaromatic hydrocarbons, including neutral and ionic examples. Subtraction of the isotropic shielding of diatomic hydrogen by itself allowed the prediction of through-space proton NMR shielding increment surfaces for these systems. Substantial shielding was observed above the center of aromatic rings, regardless of whether the ring was pi-aromatic or sigma-aromatic, and also regardless of the charge. In sharp contrast, deshielding was observed above the center of antiaromatic rings, regardless of whether the ring was pi-aromatic or sigma-aromatic, and also regardless of the charge. Shielding increment values at 2.5 angstrom above the ring centers were compared to NICS values at the same position. The shielding effects predicted by using diatomic hydrogen as a computational probe are diagnostic of whether a structure possesses aromaticity or antiaromaticity.     

Computation of through-space NMR shielding effects by functional groups common to peptides

The GIAO-HF method in Gaussian 03 was employed to calculate the isotropic shielding values of a covalently bonded hydrogen probe and to predict the through-space proton NMR shielding increment surfaces near models of simple structures containing functional groups common to peptides. The functional groups examined include the carboxylate anion, carboxylic acid, amide, amino, ammonium and guanidinium groups. Our previously developed methodology involving the use of diatomic hydrogen as a probe of through-space shielding effects was employed. Substantial shielding or deshielding effects were observed only in the cases of the charged (ionic) groups, each of which displayed shielding or deshielding effects of greater than 1 ppm at distances comparable to those observed in peptides. Equations for predicting the shielding increments of these groups as a function of the Cartesian coordinate position of the affected proton were determined. The validity of using simple structures as models of shielding by comparable functional groups in peptides was confirmed by computing the shielding effects at selected positions above a model of glycylglycylglycine and its hydrogen-bonded dimer. Knowledge of these through-space shielding effects should aid in the tertiary structure determination of peptides by NMR.