Topology of DNA G-Quadruplexes Can Be Harnessed in Holliday Junction-Based DNA Suprastructures to Control and Optimize Their Biocatalytic Properties
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F23%3A00574950" target="_blank" >RIV/68081707:_____/23:00574950 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15640/23:73621631
Result on the web
<a href="https://pubs.acs.org/doi/10.1021/acscatal.3c02818" target="_blank" >https://pubs.acs.org/doi/10.1021/acscatal.3c02818</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acscatal.3c02818" target="_blank" >10.1021/acscatal.3c02818</a>
Alternative languages
Result language
angličtina
Original language name
Topology of DNA G-Quadruplexes Can Be Harnessed in Holliday Junction-Based DNA Suprastructures to Control and Optimize Their Biocatalytic Properties
Original language description
Thenature, composition, and topology of the active sitesof bothnatural and artificial enzymes are key determinants of their catalyticperformance. While interesting structural insights have been obtainedfor natural enzymes (e.g., horseradish peroxidase, HRP), the accuratecatalytic microenvironment of HRP-mimicking DNA-based catalysts knownas G-quadruplex (GQ)/hemin DNAzymes is still unclear. Herein, we reporton a strategy allowing for fully controlling the nature of the activesite of GQ DNAzyme, precisely manipulating the composition and topologyof the hemin (Fe(III)-protoporphyrin IX) cofactor binding site. Thiswas achieved by introducing GQ within a Holliday junction (HJ) suprastructurethat enables to seize control of both the GQ folding topology (parallel,antiparallel, hybrid) and the GQ strand directionality (clockwise,counter-clockwise). By doing so, we demonstrate that the differentGQ topologies are equivalent for both hemin binding and activationand that the flanking nucleotides (dA or dTC) modulate the activationof hemin in a GQ topology-dependent manner. Our experimental findingsare supported by the most extensive molecular dynamics simulationsever been done on GQ DNAzyme, thus providing unique mechanistic insightsinto the biocatalytic activity of GQs.
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
—
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
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
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
2155-5435
Volume of the periodical
13
Issue of the periodical within the volume
16
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
10722-10733
UT code for WoS article
001040999000001
EID of the result in the Scopus database
2-s2.0-85167931445