A mechanistic study supports a two-step mechanism for peptide bond formation on the ribosome

We report the feasible pathways of the quaternary model system for the ribosome-catalyzed PT reaction obtained by density functional calculations. Our results indicate that the step from the reactant complex to the first six-membered TS involving a proton shuttle via the 2'-OH of the P-site A76...

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Veröffentlicht in:Physical chemistry chemical physics : PCCP 2013-09, Vol.15 (36), p.14931-14935
Hauptverfasser: Byun, Byung Jin, Kang, Young Kee
Format: Artikel
Sprache:eng
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Zusammenfassung:We report the feasible pathways of the quaternary model system for the ribosome-catalyzed PT reaction obtained by density functional calculations. Our results indicate that the step from the reactant complex to the first six-membered TS involving a proton shuttle via the 2'-OH of the P-site A76 in the stepwise pathway is the most favored rate-limiting step in solution. It is found that the C-O3' bond-breaking of A76 is not significant but the C-N bond formation with a tetrahedral intermediate occurs in the rate-limiting step and that the fast breakdown of the C-O3' bond is followed in the second transition state. These are consistent with recent kinetic experiments.
ISSN:1463-9076
1463-9084
DOI:10.1039/c3cp51082d