The noncovalent dimerization of a G-quadruplex/hemin DNAzyme improves its biocatalytic properties.

Chemical Science
Yu ChengCan Li

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.

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Citations

Aug 5, 2021·Journal of the American Chemical Society·Jérémie MitteauxDavid Monchaud
Dec 22, 2020·Analytical Chemistry·Shaochun JingBaoxin Li

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Methods Mentioned

BETA
electrophoresis
nuclear magnetic resonance
NMR
circular dichroism
size exclusion chromatography
biosensors

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