The noncovalent dimerization of a G-quadruplex/hemin DNAzyme improves its biocatalytic properties
Résumé
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 on a multimerization effect applied to catalytic DNAs (or DNAzymes) and demonstrate that the enzymatic proficiency of G-quadruplexes (GQs) in interaction with 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 opening new perspectives for the biotechnological applications of GQs.
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