Nitrogen Functionalities in Palladium-Catalyzed Reactions on Solid Supports: A Case Study

2006 ◽  
Vol 2006 (8) ◽  
pp. 1886-1898 ◽  
Author(s):  
Kerstin Knepper ◽  
Sylvia Vanderheiden ◽  
Stefan Bräse
2012 ◽  
Vol 8 ◽  
pp. 1191-1199 ◽  
Author(s):  
Kerstin Knepper ◽  
Sylvia Vanderheiden ◽  
Stefan Bräse

The synthesis of diverse substituted indole structures on solid supports is described. The immobilization of nitrobenzoic acid onto Merrifield resin and the subsequent treatment with alkenyl Grignard reagents delivered indole carboxylates bound to solid supports. In contrast to results in the liquid phase, ortho,ortho-unsubstituted nitroarenes also delivered indole moieties in good yields. Subsequent palladium-catalyzed reactions (Suzuki, Heck, Sonogashira, Stille) delivered, after cleavage, the desired molecules in moderate to good yields over four steps. The scope and limitations are presented.


2018 ◽  
Author(s):  
Justin Eilertsen ◽  
Santiago Schnell

<div>As a case study, we consider a coupled enzyme assay of sequential enzyme reactions obeying the Michaelis--Menten reaction mechanism. The sequential reaction consists of a single-substrate, single-enzyme non-observable reaction followed by another single-substrate, single-enzyme observable reaction (indicator reaction). In this assay, the product of the non-observable reaction becomes the substrate of the indicator reaction. A mathematical analysis of the reaction kinetics is performed, and it is found that after an initial fast transient, the sequential reaction is described by a pair of interacting Michaelis--Menten equations. Timescales that approximate the respective lengths of the indicator and non-observable reactions, as well as conditions for the validity of the Michaelis--Menten equations are derived. The theory can be extended to deal with more complex sequences of enzyme catalyzed reactions.</div>


2018 ◽  
Author(s):  
Justin Eilertsen ◽  
Santiago Schnell

<div>As a case study, we consider a coupled enzyme assay of sequential enzyme reactions obeying the Michaelis-Menten reaction mechanism. The sequential reaction consists of a single-substrate, single enzyme non-observable reaction followed by another single-substrate, single enzyme observable reaction (indicator reaction). In this assay, the product of the non-observable reaction becomes the substrate of the indicator reaction. A mathematical analysis of the reaction kinetics is performed, and it is found that after an initial fast transient, the sequential reaction is described by a pair of interacting Michaelis-Menten equations. Timescales that approximate the respective lengths of the indicator and non-observable reactions, as well as conditions for the validity of the Michaelis-Menten equations are derived. The theory can be extended to deal with more complex sequences of enzyme catalyzed reactions.</div>


Synlett ◽  
1993 ◽  
Vol 1993 (09) ◽  
pp. 680-682 ◽  
Author(s):  
Jean Pierre Genêt ◽  
Errol Blart ◽  
Monique Savignac ◽  
Stéphane Lemeune ◽  
Sandrine Lemaire-Audoire ◽  
...  

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