The noncovalent dimerization of a G-quadruplex/hemin DNAzyme improves its biocatalytic properties |
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| Authors: | Yu Cheng Mingpan Cheng Jingya Hao Guoqing Jia David Monchaud Can Li |
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| Institution: | State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023 China.; University of Chinese Academy of Sciences, Beijing 100049 China ; Institut de Chimie Moléculaire de l'' Université de Bourgogne (ICMUB), CNRS UMR 6302, UBFC Dijon, 21078 Dijon France |
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| Abstract: | While many protein enzymes exert their functions through multimerization, which improves both selectivity and activity, this has not yet been demonstrated for other naturally occurring catalysts. Here, we report a multimerization effect applied to catalytic DNAs (or DNAzymes) and demonstrate that the enzymatic efficiency of G-quadruplexes (GQs) in interaction with the hemin cofactor is remarkably enhanced by homodimerization. The resulting non-covalent dimeric GQ–DNAzyme system provides hemin with a structurally defined active site in which both the cofactor (hemin) and the oxidant (H2O2) are activated. This new biocatalytic system efficiently performs peroxidase- and peroxygenase-type biotransformations of a broad range of substrates, thus providing new perspectives for biotechnological application of GQs.Cofactor hemin is sandwiched between 3′ homodimeric G-quadruplexes, leading to an excellent DNAzyme as a mimic of peroxidase and monooxygenase. |
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