The deprotonation of the zinc-bound water and the zinc-bound bicarbonate which arose from hydration of CO2 have been simulated in vitro according to the proposed mechanism for carbonic anhydrase, with the model complex of its own active site, [LZn(OH2)]2+, where L = tris(2-benzimidazolylmethyl)amine.

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Zinc complexes of histidine-containing peptide derived from N,N′-dihistidylethylenediamine L1 and im-bzl-N,N″-dihistidyldiethylenetriamine L2 were designed and examined as catalysts for hydrolyses of bis(p-nitrophenyl)phosphate (BNPP) and p-nitrophenyl phosphate (NPP). The zinc complex of L1 was inactive and another L2 complex hydrolyzed efficiently BNPP and NPP: their pseudo-first-order rate constants are 1.1 × 10−5 s−1 and 2.1 × 10−5 s−1, respectively.