The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again

The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again

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http://www.wikidata.org/entity/Q57482468
A strategically positioned cation is crucial for efficient catalysis by chorismate mutaseTyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutaseChemistry and biology of the caged Garcinia xanthones.Kinetic evidence of an apparent negative activation enthalpy in an organocatalytic process.Toward a symphony of reactivity: cascades involving catalysis and sigmatropic rearrangementsBacillus subtilis chorismate mutase is partially diffusion-controlled.The Cation-π Interaction in Small-Molecule Catalysis.Synthesis and evaluation of caged Garcinia xanthones.Probing protein environment in an enzymatic process: All-electron quantum chemical analysis combined with ab initio quantum mechanical/molecular mechanical modeling of chorismate mutase.Investigation of quantitative structure-reactivity relationships in the aliphatic Claisen rearrangement of bis-vinyl ethers reveals a dipolar, dissociative mechanism.
P2860

The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again

Item
http://www.wikidata.org/entity/Q57482468
description
wetenschappelijk artikel
@nl
наукова стаття, опублікована в травні 1996
@uk
name
The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again
@en
The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again
@nl
type
label
The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again
@en
The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again
@nl
prefLabel
The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again
@en
The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P921
P356
P1433
P1476
The Mechanism of the Claisen Rearrangement: Déjà Vu All Over Again
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P921