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- W2034111802 abstract "In the identification of a metal-binding site within enzymes, kinetic analyses based on thio-effects and Cd2+-rescues are widely used. In those analyses, kinetic studies using a phosphorothioate have been discussed on the premise that the substitution by a sulfur atom does not change the conformation of a ribozyme. However, our present NMR structural analysis demonstrates the change of the conformation at the metal-binding site by Rp-sulfur but not by Sp-sulfur substitution and warns against incautious interpretations of thio-effects and rescue phenomena in kinetic studies using a phosphorothioate. Our analysis further demonstrates that, in solution, a Cd2+ ion can interact with an Rp-phosphorothioate (in support of the controversial McKay's structure, Nature 1994, 372, 68−74) and with an Sp-phosphorothioate (in support of the controversial Scott's structure, Cell 1995, 81, 991−1002) at the metal-binding A9/G10.1 site and that, in the former case, the bound Cd2+ ion can return the ribozyme to an active conformation and rescue its enzymatic activity." @default.
- W2034111802 created "2016-06-24" @default.
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- W2034111802 date "2004-11-09" @default.
- W2034111802 modified "2023-09-25" @default.
- W2034111802 title "NMR-Based Reappraisal of the Coordination of a Metal Ion at the Pro-<i>R</i>p Oxygen of the A9/G10.1 Site in a Hammerhead Ribozyme" @default.
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- W2034111802 doi "https://doi.org/10.1021/ja0472937" @default.
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