Journal
BULLETIN OF THE CHEMICAL SOCIETY OF JAPAN
Volume 92, Issue 10, Pages 1729-1736Publisher
CHEMICAL SOC JAPAN
DOI: 10.1246/bcsj.20190157
Keywords
DNA enzyme; Heme; Peroxidase activity
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Funding
- JSPS KAKENHI [16KT0048, 17H03027]
- Bilateral Open Partnership Joint Research Project [BBD29011]
- Grants-in-Aid for Scientific Research [17H03027, 16KT0048] Funding Source: KAKEN
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Heme in the ferric state (heme(Fe3+)) binds to G-quadruplex DNAs to form stable complexes that exhibit enhanced peroxidase activities. The complexes are considered DNAzymes possessing heme as a prosthetic group (heme-DNAzymes), and have been extensively investigated as promising catalysts for a variety of applications. On ESR and stopped-flow measurements, an iron(IV)oxo porphyrin pi-cation radical known as Compound I was detected in reaction mixtures of heme-DNAzymes and hydrogen peroxide. This finding not only resolved the long-standing issue of the mechanism underlying the enhancement of the peroxidase activity of heme(Fe3+) in the scaffold of a G-quadruplex DNA, but also provided new insights as to the design of novel heme-DNAzymes.
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