The noncovalent dimerization of a G-quadruplex/hemin DNAzyme improves its biocatalytic properties. Issue 33 (12th August 2020)

• Record Type: Journal Article
• Authors: Cheng, Yu; Cheng, Mingpan; Hao, Jingya; Jia, Guoqing; Monchaud, David; Li, Can
• Is Part Of: Chemical science. Volume 11:Issue 33(2020)
• Page Start: 8846
• Page End: 8853
• Publication Date: 2020-08-12
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/d0sc02907f
• Languages: English
• ISSNs: 2041-6520

Abstract

Abstract : Cofactor hemin is sandwiched between 3′ homodimeric G-quadruplexes, leading to an excellent DNAzyme as a mimic of peroxidase and monooxygenase. 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 (H2 O2 ) 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.