Abstract
Systematic variation of individual amino acid residues within the catalytic core by means of protein engineering has turned out to be a powerful tool for the mechanistic studies of ribonucleases. The results of such studies are, however, open to alternative interpretations, since the replacement of even a single residue may affect chain folding. This, in turn, alters the geometry, non-covalent interactions and mutual orientation of the catalytically active residues to such an extent that identification of the real origin of the observed influence on rate remains uncertain. Unambiguous structure–reactivity correlations based on studies with structurally simplified chemical models may help to distinguish between alternative mechanisms. The present review is aimed at summarizing the results of such model studies. Accordingly, cleavage of RNA phosphodiester bonds by solvent-derived species, general acids and bases, metal ions, and multifunctional small molecular entities is surveyed.
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