Specificity of a DNA-based (DNAzyme) peroxidative biocatalyst.
A complex formation between hemin and a congruous oligonucleotide not only greatly enhances the former's peroxidative activity but also results in a biocatalyst (DNAzyme) with a novel specificity. Herein substrate, regio-, enantiomeric, and diastereomeric selectivities of heme, the DNAzyme, and the enzyme horseradish peroxidase are comparatively examined.
Rojas
Antonia M
AM
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Gonzalez
Pedro A
PA
Antipov
Eugene
E
Klibanov
Alexander M
AM
D002384:Catalysis; D021881:DNA, Catalytic / Q000737:chemistry / Q000378:metabolism*; D006427:Hemin / Q000737:chemistry; D006735:Horseradish Peroxidase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000737:chemistry / Q000378:metabolism; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D009841:Oligonucleotides / Q000737:chemistry*; D010084:Oxidation-Reduction; D013379:Substrate Specificity
D021881:DNA, Catalytic; D009841:Oligonucleotides; D006427:Hemin; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase