About John Richard's Research Group
Research in John Richard's laboratory focuses on the mechanisms of enzyme-catalyzed reactions and
the reactions of small molecules in solution that may provide insight into
enzyme catalysis. This work poses many different questions related to
organic reactivity, the characterization of polar intermediates of organic
reactions and the mechanism for catalysis of formation of these
intermediates by enzymes. It provides a bridge between chemical studies
designed to characterize the reactive intermediates of organic reactions in
water and biological studies on enzymatic catalysis of these reactions.
Only tough questions are addressed, and the answers provided are generally
of great interest to the chemical community. Students in Richard's lab are
carefully mentored as they learn to think and work independently and
receive training in all of the most important experimental methods and
Many problems are under investigation and progress leading to significant
publications has been made on the following:
- Formation and Stability of Carbocations and Mechanisms for Carbocation-Nucleophile Combination.
- Mechanism of Enzymatic Catalysis of Glycosyl Transfer: b-Galactosidase.
- Formation and stability of Simple Quinone Methides.
- Dynamics for Reactions of Ion Pairs in Water.
- Formation and Stability of Carbanions in Water and the Mechanism for Proton Transfer at Carbon.
- Formation and Stability of Zwitterionic Amino-Acid Enolates.
- Mechanism of Enzymatic Catalysis of Proton Transfer: Triosephosphate Isomerase.
- Catalysis of Proton and Hydride Transfer by Metal Cations.
- Catalysis of Hydrolysis of Phosphate Diesters by Mono and Dinuclear Metal Ion Complexes.
There are strong links between these many separate problems so that work in
one area also provide insight into other problems under investigation in
the lab. This is particularly true for the results of studies on reactive
intermediates, which are directly relevant to the mechanism of action of
enzymes that catalyze formation of these intermediates.
Former coworkers in Richard's laboratory have taken industrial positions at Pfizer, Amgen and Apotech, and faculty positions in the US (Illinois State University, Eastern Kentucky University, Alice Lloyd College and Catawba College), England (Durham University), Spain (Universidad de Santiago), India (Osmania University, Hyderabad), Japan (Kurume National College of Technology) and China (Beijing University).
Professor John P. Richard
University at Buffalo
Department of Chemistry
633 Natural Sciences Complex
Buffalo, NY 14260-3000
Phone: (716) 645-6800 ext. 2194
Fax: (716) 645-6963
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Binding interactions of the phosphate group of substrate have been shown to be directly utilized in the stabiization of the transition state for the reactions catalyzed by orotidine monophosphate decarboxylase in JACS 127, 15708-15709 (2005) View pdf file ] and by triosphosphate isomerase in Biochemistry, 46, 5841-5854 (2007) [View pdf]
The effect of the coenzyme pyridoxal on the carbon acidity of amino acids and been thoroughly characterized and the relevance to enzyme catalysis discussed in JACS, 128, 3013-3021 (2007) [View pdf file]
A novel bonding interaction between ammmonia and the benzene radical cation has been probed in J. Phys. Chem. A 111, ASAP (2007) [View pdf file]
Marcus theory has been tested for a simpe proton transfer reaction in JACS 128, 6952-6961 (2007) [View pdf file]
The borderline region between stepwise and concerted solvolysis reactions has been defined with unparalled clarity in JACS, 128, 17139-17146 (2006) [View pdf file]
Richard will be a Discussion Leader at the 2007 Gordon Research Conference on Physical Organic Chemistry June 24 - 29, 2007. Registration at this excellent Conference organized by Stan Brown is strongly encouraged. [Physical Organic GRC]
Richard will be speaking at the XIth European Symposium on Organic Reactivity (ESOR XI), Faro, Portugal, July 2- 7 2007. [View Faro 2007]
Richard will be speaking at the 234th ACS Meeting, Boston MA, August 19 - 23 [View Boston ACS]