Advances in Physical Organic Chemistry
- 1st Edition, Volume 40 - March 26, 2012
- Editor: John P. Richard
- Language: English
- Hardback ISBN:9 7 8 - 0 - 1 2 - 0 3 3 5 4 0 - 4
- Paperback ISBN:9 7 8 - 0 - 1 2 - 3 9 0 9 5 7 - 2
- eBook ISBN:9 7 8 - 0 - 0 8 - 0 4 5 8 1 9 - 9
Advances in Physical Organic Chemistry provides the chemical community with authoritative and critical assessments of the many aspects of physical organic chemistry. The field is… Read more
Advances in Physical Organic Chemistry provides the chemical community with authoritative and critical assessments of the many aspects of physical organic chemistry. The field is a rapidly developing one, with results and methodologies finding applications from biology to solid state physics.
This text is ideal for those interested in the relationship between the structure and function of organic compounds, including physical and theoretical chemists as well as organic and bioorganic chemists.
For those interested in the relationship between the structure and function of organic compounds and includes physical and theoretical chemists as well as organic and bioorganic chemists
Preface (J.P. Richard). Carbenes Generated within Cyclodextrins and Zeolites (U.H. Brinker, M.G. Rosenberg). Mechanistic Studies on Enzyme-Catalyzed Phosphoryl Transfer (A. Hengge). Finite Assemblies in the Organic Solid State: Towards Engineering Properties of Solids (T.D. Hamilton, L.R. MacGillivray). The Physical Organic Chemistry of Very High-Spin Polyradicals (A. Rajca). Computer Simulation of Enzyme Catalysis and its Relationship to Physical Organic Chemistry (A. Warshel et al.). Mechanisms of Hydrolysis and Rearrangements of Arene Epoxides (D. Whelan).
- Edition: 1
- Volume: 40
- Published: March 26, 2012
- Language: English
JR
John P. Richard
John Richard received his Ph.D. from Ohio State University, under the direction of Perry Frey. His thesis reported the synthesis of chiral oxygen-18 labelled phosphorothioate analogs of adenine nucleotides, and their use to determine the stereochemical course for enzyme-catalyzed phosphoryl transfer reactions. He worked as a postdoctoral fellow at Brandeis University with Bill Jencks, and developed an azide ion clock to measure the lifetimes of carbocation intermediates of solvolysis reactions. This clock was used to show that the mechanism for nucleophilic substitution reactions at ring-substituted 1 phenylethyl derivatives is controlled by the lifetimes of the carbocation intermediates of the solvolysis reaction. He began his independent career at the Department of Chemistry at the University of Kentucky in 1985 and moved to SUNY Buffalo in 1993.
Richard is interested in understanding the mechanism for the reactions of small molecules in water, and for their catalysis by enzymes. His early independent studies focused on developing methods to determine rate and equilibrium constants for reactions of simple carbanions and carbocations intermediates of organic reactions in water. This led to a broad characterization of substituent effects on the stability of these intermediates, and a rationale for the observation that many polar electron-withdrawing substituents cause a decrease in both the stability and reactivity of resonance stabilized carbocations. Richard transitioned to studies on the mechanism for small molecule catalysis in models for enzyme-catalyzed reactions. These included proton transfer, hydride transfer, aldol condensation reactions, and phosphate diester hydrolysis. Most recently he has focused on determining the mechanism for the stabilization of reactive carbocation and carbanion enzymatic reaction intermediates through interactions with active-site protein side chains. An important outcome of this work is the determination that the most proficient enzyme catalysts of metabolic reactions utilize substrate binding interactions as glue in the construction of protein-substrate cages that provide a tremendous stabilization of carbanion and carbocation reaction intermediates. These results provide a simple rational for the existence of enzyme catalysts that follow Koshland's induced-flt mechanism.
Affiliations and expertise
Department of Chemistry, University of Buffalo, NY, USARead Advances in Physical Organic Chemistry on ScienceDirect