Ronald Kluger

Professor - Organic and Biological Chemistry

Department of Chemistry, University of Toronto, 80 St. George Street Toronto, Ontario, Canada M5S 3H6

E-mail:

 

Phone: (416)-978-3582

Office: Davenport Building 444

Laboratories: Davenport Building 450 and 451

CV -brief

 

Research Interests

o                           The site-specific modification of proteins and enzymes by designed organic compounds is an area of growing importance. We have developed new methods to modify the oxygen-carrier protein, hemoglobin, so it can be used for a number of applications. For example, we have produced multifunctional reagents that cross-link hemoglobin at specific sites, introducing properties that make the material suitable to be used as an alternative for red cells in blood transfusions. We extended the method to include ways to combine cross-linking within a protein and connecting with a second (or additional) protein. This permits the interactions of assembled proteins to be studied in a defined system.

Connecting and cross-linking two hemoglobins

 

lower route is slow - accelerated by enzyme

 

 

 

Reactions are selectively catalyzed by lanthanides (recognition of diol in water)

Aminoacylation of RNA

 

 Learn more about this with a slide presentation: click here

Selected Publications (by Area)

Overview

The article summarizes the origins of current research as well as earlier activities.

CIC Medal Award Lecture: Molecular keystones: Lessons from bioorganic reaction mechanisms  Ronald Kluger Can. J. Chem. 2006 84 1093-1105

Selective Alteration of Proteins

Chemical alterations permit systematic studies of proteins that would dissociate - these have many applications.

Acyl phosphate monoesters as biomimetic reagents

Acyl phosphate esters occur in nature but their use as reagents has been developed in our lab. They have very useful properties, especially as electrophiles in water.

Catalyzed decarboxylation: thiamin intermediates and other mechanisms

Thiamin promotes reactions in patterns that reflect those of related enzymes. The role of the protein is clear if they are compared side by side. There are remarkable differences. Our results have led us to reconsider the role of thiamin in enzyme-catalyzed decarboxylation as well as the general process with other catalysts.

Additional papers are available - we can send you more information or discuss individual interests of prospective students.

Group members and their research areas:

Name

Area

Chung-Woo Fung (Technical assistant)

instrumentation, HPLC, mass spectrometry

Sohyoung Her Aminoacylation of RNA
Raj Dhiman Lanthanide catalyzed acylation of sugars

Adelle Vandersteen

Link structure and cooperativity in hemoglobin

Dr. Ying Yang Connections in hemoglobin
Francine Lui Reactions of altered hemoglobin with nitrite
Scott Mundle 13-C kinetic isotope effects in thiamin intermediates

 

Last updated December 16, 2009

Presentations hemox manual


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