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- W2108509653 abstract "To study the interaction and the role of the metal ion in the reaction catalyzed by Escherichia coli ribonuclease HI (E. coli RNase HI), substrate analogues containing a phosphorothioate linkage or 2'-modified nucleosides at the cleavage site were used. In the presence of Mg2+ Mn2+, Co2+, Zn2+, or Cd2+, the phosphorothioate linkage with the Rp-configuration was cleaved, while the iSp-isomer was not. Kinetic studies showed that Mn2+ and Cd2+ facilitated the cleavage of the phosphorothioate to only a small extent, which indicated the absence of an interaction between the metal ion and this phosphate residue. The interaction of the metal ion with the 2-functional group was analyzed by Mg2+-titration experiments using the -OH, -NH2, and -F substrates. From Hill plots, it was found that the Kmg values were almost the same. These results are evidence of an interaction between Mg2+ and the 2'-functional group by the formation of an outer-sphere complex with a water molecule. The Hill coefficient of 1.0 for the -OH substrate indicated that a single Mg2+ ion is required for the catalysis." @default.
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- W2108509653 date "1994-12-01" @default.
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- W2108509653 title "Role of the Mg2+Ion in the Escherichia coli Ribonuclease HI Reaction" @default.
- W2108509653 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a124682" @default.
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