How Proximal Nucleobases Regulate the Catalytic Activity of G-Quadruplex/Hemin DNAzymes
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F18%3A00501656" target="_blank" >RIV/68081707:_____/18:00501656 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1021/acscatal.8b03811" target="_blank" >http://dx.doi.org/10.1021/acscatal.8b03811</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acscatal.8b03811" target="_blank" >10.1021/acscatal.8b03811</a>
Alternative languages
Result language
angličtina
Original language name
How Proximal Nucleobases Regulate the Catalytic Activity of G-Quadruplex/Hemin DNAzymes
Original language description
G-quadruplexes (G4s) are versatile catalytic DNAs when combined with hemin. Despite the repertoire of catalytically competent G4/hemin complexes studied so far, little is known about the detailed catalytic mechanism of these biocatalysts. Herein, we have carried out an in-depth analysis of the hemin binding site within the G4/hemin catalysts, providing the porphyrinic cofactor with a controlled nucleotidic environment. We intensively assessed the position-dependent catalytic enhancement in model reactions and found that proximal nucleobases enhance the catalytic ability of the G4/hemin complexes. Our results allow for revisiting the mechanism of the G4/hemin-based catalysis, especially gaining insights into the rate-limiting step, demonstrating how both the G4 core and the proximal nucleotides dA and/or dC concomitantly activate the Compound 0> 0* prototropic cleavage of H2O2 to foster Compound 1 formation. These results provide mechanistic clues as to how the properties of G4-based catalysts can be improved to ultimately make them competitive with proteinaceous enzymes.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ACS Catalysis
ISSN
2155-5435
e-ISSN
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Volume of the periodical
8
Issue of the periodical within the volume
12
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
11352-11361
UT code for WoS article
000453491100037
EID of the result in the Scopus database
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