Dataset Information

Cation clock permits distinction between the mechanisms of ?- and ?-O- and ?-C-glycosylation in the mannopyranose series: evidence for the existence of a mannopyranosyl oxocarbenium ion.

ABSTRACT: The use of a cationic cyclization reaction as a probe of the glycosylation mechanism has been developed and applied to the 4,6-O-benzylidene-protected mannopyranoside system. Cyclization results in the formation of both cis- and trans-fused tricyclic systems, invoking an intermediate glycosyl oxocarbenium ion reacting through a boat conformation. Competition reactions with isopropanol and trimethyl(methallyl)silane are interpreted as indicating that ?-O-mannosylation proceeds via an associative S(N)2-like mechanism, whereas ?-O-mannosylation and ?-C-mannosylation are dissociative and S(N)1-like. Relative rate constants for reactions going via a common intermediate can be estimated.

SUBMITTER: Huang M

PROVIDER: S-EPMC3448556 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Cation clock permits distinction between the mechanisms of α- and β-O- and β-C-glycosylation in the mannopyranose series: evidence for the existence of a mannopyranosyl oxocarbenium ion.

Huang Min M Retailleau Pascal P Bohé Luis L Crich David D

Journal of the American Chemical Society 20120831 36

The use of a cationic cyclization reaction as a probe of the glycosylation mechanism has been developed and applied to the 4,6-O-benzylidene-protected mannopyranoside system. Cyclization results in the formation of both cis- and trans-fused tricyclic systems, invoking an intermediate glycosyl oxocarbenium ion reacting through a boat conformation. Competition reactions with isopropanol and trimethyl(methallyl)silane are interpreted as indicating that β-O-mannosylation proceeds via an associative ...[more]

PMID: 22920536

Similar Datasets

Project description:The ion atmosphere is a critical structural, dynamic, and energetic component of nucleic acids that profoundly affects their interactions with proteins and ligands. Experimental methods that "count" the number of ions thermodynamically associated with the ion atmosphere allow dissection of energetic properties of the ion atmosphere, and thus provide direct comparison to theoretical results. Previous experiments have focused primarily on the cations that are attracted to nucleic acid polyanions, but have also showed that anions are excluded from the ion atmosphere. Herein, we have systematically explored the properties of anion exclusion, testing the zeroth-order model that anions of different identity are equally excluded due to electrostatic repulsion. Using a series of monovalent salts, we find, surprisingly, that the extent of anion exclusion and cation inclusion significantly depends on salt identity. The differences are prominent at higher concentrations and mirror trends in mean activity coefficients of the electrolyte solutions. Salts with lower activity coefficients exhibit greater accumulation of both cations and anions within the ion atmosphere, strongly suggesting that cation-anion correlation effects are present in the ion atmosphere and need to be accounted for to understand electrostatic interactions of nucleic acids. To test whether the effects of cation-anion correlations extend to nucleic acid kinetics and thermodynamics, we followed the folding of P4-P6, a domain of the Tetrahymena group I ribozyme, via single-molecule fluorescence resonance energy transfer in solutions with different salts. Solutions of identical concentration but lower activity gave slower and less favorable folding. Our results reveal hitherto unknown properties of the ion atmosphere and suggest possible roles of oriented ion pairs or anion-bridged cations in the ion atmosphere for electrolyte solutions of salts with reduced activity. Consideration of these new results leads to a reevaluation of the strengths and limitations of Poisson-Boltzmann theory and highlights the need for next-generation atomic-level models of the ion atmosphere.

Dataset Information

Cation clock permits distinction between the mechanisms of ?- and ?-O- and ?-C-glycosylation in the mannopyranose series: evidence for the existence of a mannopyranosyl oxocarbenium ion.

Publications

Cation clock permits distinction between the mechanisms of α- and β-O- and β-C-glycosylation in the mannopyranose series: evidence for the existence of a mannopyranosyl oxocarbenium ion.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets