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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Catalysis
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DNA, Catalytic / chemistry
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DNA, Catalytic / metabolism*
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Hemin / chemistry
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Horseradish Peroxidase / metabolism
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Hydrogen Peroxide / chemistry
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Hydrogen Peroxide / metabolism
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Molecular Structure
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Nucleic Acid Conformation
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Oligonucleotides / chemistry*
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Oxidation-Reduction
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Substrate Specificity
Substances
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DNA, Catalytic
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Oligonucleotides
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Hemin
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Hydrogen Peroxide
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Horseradish Peroxidase