Publications by authors named "Shota Hagiwara"
Heme binds to a parallel-stranded G-quadruplex DNA to form a peroxidase-mimicking heme-DNAzyme. An interpolyelectrolyte complex between the heme-DNAzyme and a cationic copolymer possessing protonated amino groups was characterized and the peroxidase activity of the complex was evaluated to elucidate the effect of the polymer on the catalytic activity of the heme-DNAzyme. We found that the catalytic activity of the heme-DNAzyme is enhanced through the formation of the interpolyelectrolyte complex due to the general acid catalysis of protonated amino groups of the polymer, enhancing the formation of the iron(IV)oxo porphyrin π-cation radical intermediate known as Compound I.
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- - The catalytic cycle of a heme-DNAzyme involves a key intermediate, an iron(IV)oxo compound, created through the breaking of an O-O bond from a hydroperoxo ligand, similar to the functioning of heme enzymes like horseradish peroxidase (HRP).
- - Research included testing chemically modified hemes with different electron densities and parallel-stranded G-quadruplex DNAs to study how these factors impact the catalytic activity of the heme-DNAzyme.
- - Results showed that the DNAzyme's activity can be boosted by increasing the electron density of the heme and utilizing surrounding adenine bases, clarifying the relationship between the heme structure and its functional performance.