Kinetic Evidence of an Apparent Negative Activation Enthalpy in an Organocatalytic Process

A combined kinetic and computational study on our tryptophan-based bifunctional thiourea catalyzed asymmetric Mannich reactions reveals an apparent negative activation enthalpy. The formation of the pre-transition state complex has been unambiguously confirmed and these observations provide an exper...

Full description

Saved in:
Bibliographic Details
Published inScientific reports Vol. 3; no. 1; p. 2557
Main Authors Han, Xiao, Lee, Richmond, Chen, Tao, Luo, Jie, Lu, Yixin, Huang, Kuo-Wei
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 30.08.2013
Nature Publishing Group
Subjects
639/638/563/979
639/638/77/883
639/638/77/885
639/638/77/889
Binding Sites
Catalysis
Computer applications
Computer Simulation
Enantiomers
Energy Transfer
Enthalpy
Entropy
Enzymes
Humanities and Social Sciences
Hydrogen
Hydrogen Bonding
Kinetics
Models, Chemical
multidisciplinary
Protein Binding
Science
Temperature
Thiourea
Thiourea - chemistry
Tryptophan
Tryptophan - chemistry
Online AccessGet full text

Cover

More Information
Summary:A combined kinetic and computational study on our tryptophan-based bifunctional thiourea catalyzed asymmetric Mannich reactions reveals an apparent negative activation enthalpy. The formation of the pre-transition state complex has been unambiguously confirmed and these observations provide an experimental support for the formation of multiple hydrogen bonding network between the substrates and the catalyst. Such interactions allow the creation of a binding cavity, a key factor to install high enantioselectivity.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
ISSN:2045-2322
2045-2322
DOI:10.1038/srep02557