4.6 Review

Development of the aza-crown ether metal complexes as artificial hydrolase

Journal

JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 154, Issue -, Pages 89-102

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2015.09.011

Keywords

Aza-crown ethers; Metal complexes; Hydrolase; Synthesis; Catalysis

Funding

  1. Chinese National Natural Science Foundation [21173274]
  2. Key Laboratory of Green Catalysis of Sichuan Institutes of High Education [LYJ14201]
  3. Natural Science Foundation Project of Chongqing [CSTC2013jcyjA50012]
  4. Chongqing Municipal Education Commission [KJ130820]
  5. Chongqing University of Technology [YCX2014217]

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Hydrolases playa crucial role in the biochemical process, which can catalyze the hydrolysis of various compounds like carboxylic esters, phosphoesters, amides, nucleic acids, peptides, and so on. The design of artificial hydrolases has attracted extensive attention due to their scientific significance and potential applications in the field of gene medicine and molecular biology. Numerous macrocyclic metal complexes have been used as artificial hydrolase in the catalytic hydrolysis of the organic substrate. Aza-crown ether for this comment is a special class of the macrocyclic ligand containing both the nitrogen atoms and oxygen atoms in the ring. The studies showed that the aza-crown complexes exhibited high activity of hydrolytic enzyme. However, the aza-crown ether metal complex as artificial hydrolase is still very limited because of its difficulty in synthesis. This review summarizes the development of the aza-crown ether metal complexes as the artificial hydrolase, including the synthesis and catalysis of the transition metal complexes and lanthanide metal complexes of aza-crown ethers. The purpose of this review is to highlight: (1) the relationship between the structure and hydrolytic activity of synthetic hydrolase; (2) the synergistic effect of metal sites and ligands in the course of organic compound hydrolysis; and (3) the design strategies of the aza-crown ethers as hydrolase. (C) 2015 Elsevier Inc. All rights reserved.

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