Observations on catalysis by hammerhead ribozymes are consistent with a two-divalent-metal-ion mechanism
Pontius, B. W., Lott, W. B., & von Hippel, P. H. (1997) Observations on catalysis by hammerhead ribozymes are consistent with a two-divalent-metal-ion mechanism. Proceedings of the National Academy of Sciences of the United States of America, 94(6), pp. 2290-4.
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Significant cleavage by hammerhead ribozymes requires activation by divalent metal ions. Several models have been proposed to account for the influence of metal ions on hammerhead activity. A number of recent papers have presented data that have been interpreted as supporting a one-metal-hydroxide-ion mechanism. In addition, a solvent deuterium isotope effect has been taken as evidence against a proton transfer in the rate-limiting step of the cleavage reaction. We propose that these data are more easily explained by a two-metal-ion mechanism that does not involve a metal hydroxide, but does involve a proton transfer in the rate-limiting step.
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|Item Type:||Journal Article|
|Additional Information:||Pontius, B W Lott, W B von Hippel, P H GM-15792/GM/NIGMS NIH HHS/United States GM-29158/GM/NIGMS NIH HHS/United States Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. United states Proceedings of the National Academy of Sciences of the United States of America Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2290-4.|
|Keywords:||Base Sequence, Binding Sites, Calcium, Catalysis, *Cations, Divalent, Cobalt, Crystallography, X-Ray, Kinetics, Lead, Magnesium, Manganese, Molecular Sequence Data, Nucleic Acid Conformation, RNA, Catalytic/*chemistry/*metabolism, Thionucleotides|
|Divisions:||Current > Schools > School of Chemistry, Physics & Mechanical Engineering|
Current > Institutes > Institute of Health and Biomedical Innovation
Current > QUT Faculties and Divisions > Science & Engineering Faculty
|Copyright Owner:||Copyright 1997 National Academy of Sciences of the USA|
|Deposited On:||26 Jul 2012 16:11|
|Last Modified:||26 Jul 2012 16:13|
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