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2019, Vol.92, No.10

1729-1736

Identification of Intermediates in Peroxidase Catalytic Cycle of a DNAzyme Possessing Heme

Ryosuke Shinomiya ,1Haruka Araki ,1Atsuya Momotake ,1Hiroaki Kotani ,1Takahiko Kojima ,1 and Yasuhiko Yamamoto *1,2,3
1Department of Chemistry, University of Tsukuba, Tsukuba, Ibaraki 305-8571, Japan
2Tsukuba Research Center for Energy Materials Science (TREMS), University of Tsukuba, Tsukuba, Ibaraki 305-8571, Japan
3Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Tsukuba, Ibaraki 305-8577, Japan
https://doi.org/10.1246/bcsj.20190157

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Abstract

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 π-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.

figure

An iron(IV)oxo porphyrin π-cation radical known as Compound I was detected in reaction mixtures of heme-DNAzymes and hydrogen peroxide.

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