Ribonucleases and small nucleolytic ribozymes are both able to catalyze RNA strand cleavage through 2'--transphosphorylation, provoking the question of whether protein and RNA enzymes facilitate mechanisms that pass through the same or distinct transition states. Here, we report the primary and secondary O kinetic isotope effects for hepatitis delta virus ribozyme catalysis that reveal a dissociative, metaphosphate-like transition state in stark contrast to the late, associative transition states observed for reactions catalyzed by specific base, Zn ions, or ribonuclease A. This new information provides evidence for a discrete ribozyme active site design that modulates the RNA cleavage pathway to pass through an altered transition state.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10112047 | PMC |
| http://dx.doi.org/10.1021/jacs.2c10079 | DOI Listing |
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