Probing the limits of rate acceleration mediated by hydrogen bonds

被引：11

作者：

Cowie, Rosalyne M.

Turega, Simon M.

Philp, Douglas

机构：

[1] Univ St Andrews, EaStCHEM, St Andrews KY16 9ST, Fife, Scotland

[2] Univ St Andrews, Ctr Biomol Sci, Sch Chem, St Andrews KY16 9ST, Fife, Scotland

来源：

ORGANIC LETTERS | 2006年 / 8卷 / 23期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1021/ol061290c

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

A simple receptor and substrate are used to probe the relationship between transition-state charge and the level of rate acceleration that can be created by stabilizing the transition state through hydrogen bonding. Pericyclic reactions are accelerated less than 2-fold by the receptor, whereas a conjugate addition reaction is accelerated more than 30-fold. Therefore, substrate polarization by hydrogen bonding would only appear to be effective for reactions that generate significant charge at the transition state.

引用

收藏

页码：5179 / 5182

页数：4

相关论文

共 35 条

[1] Lovastatin nonaketide synthase catalyzes an intramolecular Diels-Alder reaction of a substrate analogue [J].

Auclair, K ;

Sutherland, A ;

Kennedy, J ;

Witter, DJ ;

Van den Heever, JP ;

Hutchinson, CR ;

Vederas, JC .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (46) :11519-11520

[2] Recognition-mediated facilitation of a disfavored Diels-Alder reaction [J].

Bennes, R ;

Philp, D ;

Spencer, N ;

Kariuki, BM ;

Harris, KDM .

ORGANIC LETTERS, 1999, 1 (07) :1087-1090

[3] Efficient recognition-induced acceleration of a [3+2] dipolar cycloaddition reaction [J].

Booth, CA ;

Philp, D .

TETRAHEDRON LETTERS, 1998, 39 (38) :6987-6990

[4] AN ANTIBODY-CATALYZED OXY-COPE REARRANGEMENT [J].

BRAISTED, AC ;

SCHULTZ, PG .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1994, 116 (05) :2211-2212

[5]

Desimoni G., 1983, J AM CHEM SOC

[6]

Fan EK, 1997, NEW J CHEM, V21, P81

[7] Salicylate biosynthesis in Pseudomonas aeruginosa -: Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities [J].

Gaille, C ;

Kast, P ;

Haas, D .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (24) :21768-21775

[8] Bioorganic route to Hetero-Diels-Alder products [J].

Gouverneur, V ;

Reiter, M .

CHEMISTRY-A EUROPEAN JOURNAL, 2005, 11 (20) :5806-5815

[9] CONTROL OF THE EXO-PATHWAY AND ENDO-PATHWAY OF THE DIELS-ALDER REACTION BY ANTIBODY CATALYSIS [J].

GOUVERNEUR, VE ;

HOUK, KN ;

DEPASCUALTERESA, B ;

BENO, B ;

JANDA, KD ;

LERNER, RA .

SCIENCE, 1993, 262 (5131) :204-208

[10] Macrophomate synthase: QM/MM simulations address the Diels-Alder versus Michael-Aldol reaction mechanism [J].

Guimaraes, CRW ;

Udier-Blagovic, M ;

Jorgensen, WL .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (10) :3577-3588

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