Richard, John P. - University at Buffalo, the State University of New York

个人简介

B.S., Ohio State University (1974) Ph.D., Ohio State University (1979) Postdoctoral Fellow, Brandeis University (1979-82) Research Associate, Fox Chase Cancer Center (1982-84) Herchel Smith Fellow in Organic Chemistry, Cambridge University, Cambridge, England (1984-85) Honors and Awards: Herchel Smith Fellowship, University of Cambridge, United Kingdom, 1984-1985. NIH First Award, 1988. NSF Special Creativity Award, 2007. 2003 T S. Walton Visitor, University College Dublin, Ireland, 2003. Visiting Professor of Chemistry, Departamento de Química Física, Universidad de Santiago, Spain, August 2003, 2006, 2009 and 2011. Visiting Professor of Chemistry, Department Chemie, Ludwig-Maximilians-Universität Muenchen, Germany, 2004 and 2010. Editorial Board of Bioorganic Chemistry, 1998 – present. Editorial Board of The Journal of Physical Organic Chemistry, 2003 – present. Editorial Board of Biochemistry, 2010 – present. Coeditor of Annual Reports on the Progress of Chemistry: Organic Chemistry, 1996-2002. Editor of Advances in Physical Organic Chemistry, 2000-2012. Secretary, Division of Biological Chemistry, American Chemical Society, 2003-2008. Co-Chair Gordon Research Conference on Enzymes, Coenzymes and Metabolic Pathways, 2006. Chair Gordon Research Conference on Isotopes in Chemistry and Biology, 2010. Chair of the Organizing Committee for the 22nd Enzyme Mechanisms Conference, 2011. Organizing Committee, Reaction Mechanisms VII Conference, Dublin, Ireland, 2004. Advisory Board, IUPAC 19th International Conference on Physical Organic Chemistry, ICPOC-17, 18 and 19, 2006, 2008, 2010. Jacob Schoellkopf Medal (ACS Western New York Section), 2009. UB Distinguished Professor of Chemistry, 2012. Fellow of the American Chemical Society, 2014.

研究领域

The field of molecular biology requires a community of biologists who possess an intuitive understanding of how to delineate the many complex cellular and higher-order processes which occur in living systems, and of chemists and biochemists who possess the ability to determine the underlying chemical mechanism for these biological processes. Within the latter community studies of enzymes and their reaction mechanisms have long provided a unique understanding of how life functions at a molecular level. There are many questions that can be raised about the mechanism for uncatalyzed and enzyme-catalyzed reactions of small molecules in water. What are the lifetimes of carbanion and carbenium ion intermediates of these reactions, and how does their lifetime govern the reaction mechanism? Why are some reaction mechanisms stepwise and other mechanisms concerted? What imperatives determine the chemical mechanisms for enzyme-catalyzed reactions? What is the origin of the rate acceleration for enzymatic reactions. What are the intermediates of enzyme-catalyzed reactions, and how are these species stabilized by interaction with the protein catalyst? Research projects in progress at this time in Professor Richard’s lab include: (1) The determination of the rate and equilibrium constants for addition of nucleophilic reagents to simple carbenium ions and the effect of changing carbenium ion structure on these kinetic and thermodynamic parameters. (2) The generation of biologically important enolates, and development of experimental protocol to estimate the pKas for weak carbon acids. (3) Studies on the mechanism for nonenzymatic and enzyme-catalyzed aldol addition reactions in water. (4) The determination of the mechanistic imperatives for nonenzymatic and enzyme-catalyzed aldose-ketose and allylic isomerization reactions. (5) The characterization of the transition state and intermediates of b-galactosidase catalyzed hydrolysis of glycosides and determination of the function of essential amino-acid residues in the enzymatic reaction.

近期论文

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"Goryanova, T. L. Amyes, J. A. Gerlt and J. P. Richard “OMP Decarboxylase: Phosphodianion Binding Energy is Used to Stabilize a Vinyl Carbanion Reaction Intermediate”, J. Am. Chem. Soc. [Communication], 133, 6545-6548 (2011). M. Malabanan, A. P. Koudelka, T L. Amyes and J. P. Richard, “Mechanism for Activation of Triosephosphate Isomerase by Phosphite Dianion: The Role of a Hydrophobic Clamp”, J. Am. Chem. Soc., 134, 10286-10298 (2012). Jonnalagadda, K. Toth, and J. P. Richard, “Isopentenyl Diphosphate Isomerase Catalyzed Reactions in D2O: Product Release Limits the Rate of this Sluggish Enzyme-Catalyzed Reaction”, J. Am. Chem. Soc. [Communication], 134, 6568-6570 (2012). -Y. Tsang, B. M. Wood, F. M. Wong, W. Wu, J. A. Gerlt, T. L. Amyes, J. P. Richard “Proton Transfer from C-6 of Uridine 5′-Monophosphate Catalyzed by Orotidine 5′-Monophosphate Decarboxylase: Formation and Stability of a Vinyl Carbanion Intermediate and the Effect of a 5-Fluoro Substituent”, J. Am. Chem. Soc., 134, 14580-14594 (2012). M. Malabanan, L. N.-Velasquez, T L. Amyes and J. P. Richard, ” Magnitude and Origin of the Enhanced Basicity of the Catalytic Glutamate of Triosephosphate Isomerase”, J. Am. Chem. Soc., [Communication] 134, 5978-5981 (2013). L. Amyes and J. P. Richard “Specificity in Transition State Binding: The Pauling Model Revisited”, Biochemistry, 52, 2021-2035 (2013). Spong, T. L. Amyes and J. P. Richard, “Enzyme Architecture: The Activating Oxydianion Binding Domain for Orotidine 5’-Monophophate Decarboxylase”, J. Am. Chem. Soc. [Communication] 134, 18343-18346 (2013). P. Richard, T. L. Amyes, B. Goryanova and X. Zhai, “Enzyme Architecture: On the Importance of Being in a Protein Cage”, Curr. Opin. Chem. Biol., 21, 1-10 (2014). Zhai, T. L. Amyes and J. P. Richard, “Enzyme Architecture: Remarkably Similar Transition States for Triosephosphate Isomerase Catalyzed Reactions of the Whole Substrate and Substrate in Pieces”, J. Am. Chem. Soc. [Communication] 135, 4145-4148 (2014). Spotlight Article, J. Am. Chem. Soc., 135, 4595-4596 (2014). M. Goldman, T. L. Amyes, B. Goryanova, J. A. Gerlt and J. P. Richard, “Enzyme Architecture: Deconstruction of the Enzyme-Activating Phosphodianion Interactions of Orotidine 5’-Monophosphate Decarboxylase”, J. Am. Chem. Soc., 135, 10156-10165 (2014).