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Understanding the transition states of phosphodiester bond cleavage: Insights from heavy atom isotope effects by Adam G. Cassano; Vernon E. Anderson; Michael E. Harris is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The nucleotides of DNA and RNA are joined by phosphodiester linkages whose synthesis and hydrolysis are catalyzed by numerous essential enzymes. Two prominent mechanisms have been proposed for RNA and protein enzyme catalyzed cleavage of phosphodiester bonds in RNA: (a) __intra__molecular nucleophilic attack by the 2′‐hydroxyl group adjacent to the reactive phosphate; and (b) __inter__molecular nucleophilic attack by hydroxide, or other oxyanion. The general features of these two mechanisms have been established by physical organic chemical analyses; however, a more detailed understanding of the transition states of these reactions is emerging from recent kinetic isotope effect (KIE) studies. The recent data show interesting differences between the chemical mechanisms and transition state structures of the inter‐ and intramolecular reactions, as well as provide information on the impact of metal ion, acid, and base catalysis on these mechanisms. Importantly, recent nonenzymatic model studies show that interactions with divalent metal ions, an important feature of many phosphodiesterase active sites, can influence both the mechanism and transition state structure of none

Who reads Understanding the transition states of phosphodiester bond cleavage: Insights from heavy atom isotope effects?

Author

Adam G. Cassano; Vernon E. Anderson; Michael E. Harris

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

2003

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)