title: Specificity of a DNA-based (DNAzyme) peroxidative biocatalyst.
abstract: 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.
authors.affiliation: Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
authors.forename: Antonia M
authors.initials: AM
authors.lastname: Rojas
authors.forename: Pedro A
authors.initials: PA
authors.lastname: Gonzalez
authors.forename: Eugene
authors.initials: E
authors.lastname: Antipov
authors.forename: Alexander M
authors.initials: AM
authors.lastname: Klibanov
mesh_terms: 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
chemical_list: D021881:DNA, Catalytic; D009841:Oligonucleotides; D006427:Hemin; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase