Nucleophilic reaction by carbonic anhydrase model zinc compound: characterization of intermediates for CO2 hydration and phosphoester hydrolysis

A Novel Dinucleating Ligand-Containing Hexabenzimidazoles and Its Dinuclear Zinc Complex Bridged by a Carboxylate Group for the Hydrolysis of 2-Hydroxypropyl-p-nitrophenyl phosphate

“…The rate levels off at pH 8.5 indicating that the most active form of this dinuclear complex must have a hydroxide ion at one of its zinc(II) centers. The zinc(II)-bound hydroxide ion can contribute to the hydrolysis by acting as a nucleophile [27][28][29][30].…”

“…Recently, many synthetic mononuclear and dinuclear zinc(II) complexes [28][29][30][31][32] of ligands incorporating benzimidazoles have drawn much attention, because they are useful to elucidate the nature of the active site of the hydrolytic enzyme [28][29][30][31][32][33][34][35] and the catalytic mechanism.…”

“…As part of our studies in biomimetic hydrolytic zinc enzymes [28][29][30][36][37][38][39] and with the aim to mimic the key features of the two zinc(II) centers in these metalloenzymes, we designed and synthesized a dizinc(II) complex [LZn 2 ](ClO 4 ) 3 1 where L is a novel dinucleating ligand containing two tridentate tris(N-methylbenzimidazolylethyl)methane subunits bridged by carboxylate group (Scheme 1). Steric preorganization of the zinc(II) ions by the relatively rigid benzimidazole moieties facilitates the incorporation of substrate binding and catalysis.…”

Zinc(II) tweezers containing artificial peptides mimicking the active site of phosphotriesterase: The catalyzed hydrolysis of the toxic organophosphate parathion

“…Several studies have been devoted to elucidate the effect of the ligand structure in modulating the reactivity of the metal center [33][34][35][36] but it is quite clear that the desired acceleration cannot be reached with simple mononuclear complexes [37][38][39][40][41][42][43][44].…”

A family of insulinomimetic zinc(II) complexes of amino ligands with Zn(Nn) (n=3 and 4) coordination modes

“…In addition, macrocyclic Zn(II) complexes provided suitable models to mimic active sites of various zinc enzymes such as b-lactamase II, carbonic anhydrase, and alcohol dehydrogenase [10][11][12][13][14][15].…”