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        <title>Probing Metal-Dependent Phosphate Binding for the Catalysis of the 17E DNAzyme</title>
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        <namePart type="given">Woohyun</namePart>
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    <abstract>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 \textgreater900. 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.</abstract>
    <identifier type="citekey">Moon-2021-Probing</identifier>
    <identifier type="doi">10.1021/acs.biochem.1c00091</identifier>
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        <url>https://gwf-uwaterloo.github.io/gwf-publications/G21-128001</url>
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        <date>2021</date>
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        <detail type="issue"><number>24</number></detail>
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            <start>1909</start>
            <end>1918</end>
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%0 Journal Article
%T Probing Metal-Dependent Phosphate Binding for the Catalysis of the 17E DNAzyme
%A Moon, Woohyun J.
%A Huang, Po‐Jung Jimmy
%A Liu, Juewen
%J Biochemistry, Volume 60, Issue 24
%D 2021
%V 60
%N 24
%I American Chemical Society (ACS)
%F Moon-2021-Probing
%X 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 \textgreater900. 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.
%R 10.1021/acs.biochem.1c00091
%U https://gwf-uwaterloo.github.io/gwf-publications/G21-128001
%U https://doi.org/10.1021/acs.biochem.1c00091
%P 1909-1918

Markdown (Informal)

[Probing Metal-Dependent Phosphate Binding for the Catalysis of the 17E DNAzyme](https://gwf-uwaterloo.github.io/gwf-publications/G21-128001) (Moon et al., GWF 2021)

• Probing Metal-Dependent Phosphate Binding for the Catalysis of the 17E DNAzyme (Moon et al., GWF 2021)

ACL

• Woohyun J. Moon, Po‐Jung Jimmy Huang, and Juewen Liu. 2021. Probing Metal-Dependent Phosphate Binding for the Catalysis of the 17E DNAzyme. Biochemistry, Volume 60, Issue 24, 60(24):1909–1918.