Unusual metal ion catalysis in an acyl-transferase ribozyme.

@article{Suga1998UnusualMI,
  title={Unusual metal ion catalysis in an acyl-transferase ribozyme.},
  author={Hiroaki Suga and James Allan Cowan and Jack W Szostak},
  journal={Biochemistry},
  year={1998},
  volume={37 28},
  pages={10118-25}
}
Most studies of the roles of catalytic metal ions in ribozymes have focused on inner-sphere coordination of the divalent metal ions to the substrate or ribozyme. However, divalent metal ions are strongly hydrated in water, and some proteinenzymes, such as Escherichia coli RNase H and exonuclease III, are known to use metal cofactors in their fully hydrated form [Duffy, T. H., and Nowak, T. (1985) Biochemistry 24, 1152-1160; Jou, R., and Cowan, J. A. (1991) J. Am. Chem. Soc. 113, 6685-6686]. It… CONTINUE READING