6533b7d8fe1ef96bd126aee6
RESEARCH PRODUCT
The noncovalent dimerization of a G-quadruplex/hemin DNAzyme improves its biocatalytic properties.
Yu ChengYu ChengMingpan ChengJingya HaoJingya HaoDavid MonchaudGuoqing JiaCan Lisubject
[SDV.BIO]Life Sciences [q-bio]/BiotechnologyDeoxyribozyme010402 general chemistryG-quadruplex01 natural sciencesCofactor03 medical and health scienceschemistry.chemical_compoundheterocyclic compounds030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryActive siteGeneral Chemistry[CHIM.CATA]Chemical Sciences/CatalysisCombinatorial chemistry[SDE.ES]Environmental Sciences/Environmental and Society0104 chemical sciencesChemistryEnzymebiology.proteinSelectivityPeroxidaseHemindescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2020-07-15 | Chemical science |