Field
Value
Language
dc.contributor.author
Moon, Woohyun Jennifer
datacite.creator.affiliationIdentifier
https://ror.org/01aff2v68
en_US
datacite.creator.affiliation
University of Waterloo
en_US
datacite.creator.nameIdentifier
en_US
dc.contributor.author
Huang, Po-Jung Jimmy
datacite.creator.affiliationIdentifier
https://ror.org/01aff2v68
en_US
datacite.creator.affiliation
University of Waterloo
en_US
datacite.creator.nameIdentifier
https://orcid.org/0000-0003-3436-9968
en_US
dc.contributor.author
Liu, Juewen
datacite.creator.affiliationIdentifier
https://ror.org/01aff2v68
en_US
datacite.creator.affiliation
University of Waterloo
en_US
dc.coverage.temporal
2019-05-01/2021-05-31
dc.date.accessioned
2022-06-10T17:02:19Z
dc.date.available
2022-06-10T17:02:19Z
dc.date.issued
2022-06-10
dc.identifier.uri
https://www.frdr-dfdr.ca/repo/dataset/4f876e4d-d2ed-43e5-9421-623882e6a594
dc.identifier.uri
https://doi.org/10.20383/103.0588
dc.description
The RNA-cleaving 17E DNAzyme exhibits different levels of cleavage activity in the presence of various divalent metal ions, with Pb2+ giving the fastest cleavage. In this study, the metal–phosphate interaction is probed to understand the trend of activity with different metal ions. For the first-row transition metals, the lowest activity shown by Ni2+ correlates with the inhibition by the inorganic phosphate and its water ligand exchange rate, suggesting inner-sphere metal coordination. Cleavage activity with the two stereoisomers of the phosphorothioate-modified substrates, Rp and Sp, indicated that Mg2+, Mn2+, Fe2+, and Co2+ had the highest Sp:Rp activity ratio of >900. Comparatively, the activity was much less affected using the thiophilic metals, including Pb2+, suggesting inner-sphere coordination. The pH–rate profiles showed that Pb2+ was different than the rest of the metal ions in having a smaller slope and a similar fitted apparent pKa and the pKa of metal-bound water. Combining previous reports and our current results, we propose that Pb2+ most likely plays the role of a general acid while the other metal ions are Lewis acid catalysts interacting with the scissile phosphate.
en_US
dc.publisher
Federated Research Data Repository / dépôt fédéré de données de recherche
dc.rights
Creative Commons Public Domain Dedication (CC0 1.0)
en_US
dc.rights.uri
https://creativecommons.org/publicdomain/zero/1.0/
en_US
dc.subject
DNAzyme
en_US
dc.subject
Pb2+
en_US
dc.subject
Biosensor
en_US
dc.title
Probing Metal-Dependent Phosphate Binding for the Catalysis of the 17E DNAzyme
en_US
globus.shared_endpoint.name
f163c1b3-9c88-42f6-a7bb-5839ed6c4063
globus.shared_endpoint.path
/2/published/publication_583/
datacite.publicationyear
2022
datacite.resourcetype
Dataset
en_US
datacite.relatedidentifier.IsCitedBy
https://doi.org/10.1021/acs.biochem.1c00091
datacite.fundingReference.funderIdentifier
https://ror.org/01h531d29
en_US
datacite.fundingReference.funderName
Natural Sciences and Engineering Research Council of Canada (NSERC)
en_US
datacite.fundingReference.awardNumber
en_US
datacite.fundingReference.awardTitle
Canada First Research Excellence Fund
en_US
frdr.crdc.code
RDF1060101
en_US
frdr.crdc.group_en
Biological sciences
en_US
frdr.crdc.class_en
Biochemistry
en_US
frdr.crdc.field_en
Analytical biochemistry
en_US
frdr.crdc.group_fr
Sciences biologiques
fr_CA
frdr.crdc.class_fr
Biochimie
fr_CA
frdr.crdc.field_fr
Biochimie analytique
fr_CA
datacite.description.other
Dataset is from publication "Probing Metal-Dependent Phosphate Binding for the Catalysis of the 17E DNAzyme"
datacite.description.other
Item exited embargo and became publicly available on 2022-06-10
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