We have investigated the properties of cobalamin complexes with imidazolate using the density functional B3LYP method. In particular, we have compared imidazolate (Imm) with imidazole and 5,6-dimethylbenzimidazole (DMB), and studied how constraints in the axial Co–N bond length may affect the strength of the Co–C bond. The results show that the optimum Co–NImm bond is ∼0.2Å shorter than that of imidazole. There is no indication from crystal structures that the histidine ligand would be deprotonated in the enzymes. However, it is likely that it attains some imidazolate character through its hydrogen bond to a conserved aspartate residue. The Co–N bond with imidazolate is three times more rigid than that with imidazole or DMB, but twice as flexible as the Co–C bond. Constraints in the Co–NImm bond length give rise to a larger change in the corrin conformation than imidazole, but smaller than for DMB. The resulting effect for the Co–C bond dissociation energy is larger for imidazolate than for imidazole or DMB. However, even the largest reasonable distortion can only enhance catalysis by 15kJmol−1. Therefore, we conclude that, irrespective of the nature of the N-base, constraints in the axial Co–N bond lengths cannot be the main reason for the catalytic power of cobalamin enzymes.