:: Full Publications List Since 1995

The Effects of Sulfur Substitution for the Nucleophile and Bridging Oxygen Atoms in Reactions of Hydroxyalkyl Phosphate Esters, S. Iyer and A.C. Hengge. J. Org. Chem. 2008, 73, 4819-4829.

Kinetic Isotope Effects for Alkaline Phosphatase Reactions: Implications for the Role of Active-Site Metal Ions in Catalysis, J. G. Zalatan, I. Catrina, R. Mitchell, P.K. Grzyska, P.J. O'Brien, D. Herschlag and A.C. Hengge. J. Am. Chem. Soc. 2007, 129, 9789-9798.

Diesterase Activity and Substrate Binding in Purple Acid Phosphatases, R.S. Cox, G. Schenk, N. Mitic, L.R. Gahan and A.C. Hengge. J. Am. Chem. Soc. 2007, 129, 9550-9551.

Mechanism of Rhodium-Catalyzed Carbene Formation from Diazo Compounds, F.M. Wong, J. Wang, A.C. Hengge and W. Wu. Org. Lett. 2007, 9, 1663-1665.

Probing the Origin of the Compromised Catalysis of E. coli Alkaline Phosphatase in its Promiscuous Sulfatase Reaction, I. Catrina, P.J. O'Brien, J. Purcell, I. Nikolic-Hughes, J.G. Zalatan, A.C. Hengge and D. Herschlag. J. Am. Chem. Soc. 2007, 129, 5760-5765.

Enzymatic Mechanisms of Phosphate and Sulfate Transfer, W.W. Cleland and A.C. Hengge. Chem. Rev. 2006, 106, 3252-3278.

Metal-Catalyzed Phosphodiester Cleavage: Secondary ¹⁸O Isotope Effects as an Indicator of Mechanism, J. Rawlings, W.W. Cleland and A.C. Hengge. J. Am. Chem. Soc. 2006, 128, 17120-17125.

The Transition State of the Sulfuryl Transfer Reaction of Estrogen Sulfotransferase, R.H. Hoff, P.G. Czyryca, M. Sun, T.S. Leyh, and A.C. Hengge. J. Biol. Chem. 2006, 281, 30645-30649.

Thermodynamic Origin of the Increased Rate of Hydrolysis of Phosphate and Phosphorothioate Esters in DMSO/Water Mixtures, K. Sorensen-Stowell and A.C. Hengge. J. Org. Chem. 2006, 71, 7180-7184.

Transesterification Thio Effects of Phosphate Diesters: Free Energy Barriers and Kinetic and Equilibrium Isotope Effects from Density-Functional Theory, Y. Liu, B.A. Gregersen, A.C. Hengge and D.M. York. Biochemistry. 2006, 45, 10043-10053.

The Thermodynamics of Phosphate versus Phosphorothioate Ester Hydrolysis, J. Purcell and A.C. Hengge. J. Org. Chem. 2005, 70, 8437-8442.

Probing Potential Medium Effects on Phosphate Ester Bonds Using ¹⁸O Isotope Shifts on ³¹P NMR, K. Sorensen-Stowell and A.C. Hengge. J. Org. Chem. 2005, 70, 8303-8308.

Examination of P-OR Bridging Bond Orders in Phosphate Monoesters using ¹⁸O Isotope Shifts in ³¹P NMR, K. Sorensen-Stowell and A.C. Hengge. J. Org. Chem. 2005, 70, 4805-4809.

A Concerted Mechanism for the Transfer of the Thiophosphinoyl Group from Aryl Dimethylphosphinothioate Esters to Oxyanionic Nucleophiles in Aqueous Solution, I. I. Onyido, K. Swierczek, J. Purcell and A.C. Hengge. J. Am. Chem. Soc., 2005, 127, 7703-7711.

Physical Organic Perspectives on Phospho Group Transfer from Phosphates and Phosphinates, A.C. Hengge and I. Onyido. Curr. Org. Chem. 2005, 9, 61-74.

Mechanistic Studies of Protein Tyrosine Phosphatases YopH and Cdc25A with m-Nitrobenzyl Phosphate, D.F. McCain, P.K. Grzyska, L. Wu, A.C. Hengge and Z.-Y. Zhang. Biochemistry. 2004, 43, 8256-8264.

Altered mechanisms of reactions of phosphate esters bridging a dinuclear metal center, T. Humphry, M. Forconi, N.H. Williams and A.C. Hengge. J. Am. Chem. Soc. 2004, 126, 11864-11869.

A nonhydrolyzable analogue of phosphotyrosine, and related aryloxymethano- and aryloxyethano- phosphonic acids as motifs for inhibition of phosphatases, S. Iyer, J.M. Younker, P.G. Czyryca and A.C. Hengge. Bioorg. Med. Chem. Lett., 2004, 14, 5931-5935.

A Mechanistic Study of the Alkaline Hydrolysis of Diaryl Sulfate Diesters, J.M. Younker and A.C. Hengge. J. Org. Chem. 2004, 69, 9043-9048.

Probing the Transition-State Structure of Dual-Specificity Protein Phosphatases Using a Physiological Substrate Mimic, P.K. Grzyska, Y. Kim, M.D. Jackson, A.C. Hengge and J.M. Denu. Biochemistry. 2004, 43, 8807-8814.

An Investigation of the Sulfuryl Transfer Step from Substrate to Enzyme by Aryl Sulfatases, S.G. Gibby, J.M. Younker and A.C. Hengge. J. Phys. Org. Chem. 2004, 17, 541-547. Invited paper, special issue dedicated to William P. Jencks.

Role of Protein Conformational Mobility in Enzyme Catalysis - Acylation of alfa-Chymotrypsin by Specific Peptide Substrates, A.C. Hengge and R.L. Stein. Biochemistry. 2004, 43, 742-747.

Transition State Differences in Hydrolysis Reactions of Alkyl versus Aryl Phosphate Monoester Monoanions, P.K. Grzyska, P.G. Czyryca, J. Purcell and A.C. Hengge. J. Am. Chem. Soc. 2003, 125, 13106-13111.

A convenient synthesis of phosphonothioic acids, K. Swierczek, J. Peters and A.C. Hengge. Tetrahedron. 2003, 59, 595-599.

Metal ion catalyzed hydrolysis of ethyl p-nitrophenyl phosphate, J. Rawlings, W.W. Cleland and A.C. Hengge. J. Inorg. Biochem. 2003, 93, 61-65.

Comparisons of Phosphorothioate with Phosphate Transfer Reactions for a Monoester, Diester and Triester: Isotope Effect Studies, I.E. Catrina and A.C. Hengge. J. Am. Chem. Soc. 2003, 125, 7546-7552.

A Comparison of Phosphonothioic Acids with Phosphonic Acids as Phosphatase Inhibitors, K. Swierczek, A.S. Pandey, J. Peters and A.C. Hengge. J. Med. Chem. 2003, 46, 3703-3708.

Isotope Effects In the Study of Phosphoryl and Sulfuryl Transfer Reactions, A.C. Hengge. Acc. Chem. Res. 2002, 35, 105-112.

Generality of Solvation Effects on the Hydrolysis Rates of Phosphate Monoesters, and Their Possible Relevance to Enzymatic Catalysis, P.K. Grzyska, P.G. Czyryca, J. Golightly, K. Small, P. Larsen, R.H. Hoff and A.C. Hengge. J. Org. Chem. 2002, 67, 1214-1220.

The catalytic mechanism of Cdc25A phosphatase, D.F. McCain, I.E. Catrina, A.C. Hengge and Z.-Y. Zhang. J. Biol. Chem. 2002, 277, 11190-11200.

Isotope effects on enzymatic and nonenzymatic reactions of phosphorothioates, I.E. Catrina, P.G. Czyryca and A.C. Hengge. Nukleonika. 2002, 47 (Supplement 1), S17-S23.

An Altered Mechanism of Hydrolysis for a Metal-Complexed Phosphate Diester, T. Humphry, M. Forconi, N.H. Williams and A.C. Hengge. J. Am. Chem. Soc. 2002, 124, 14860-14861.

Transition state analysis and requirement of Asp-262 general acid/base catalyst for full activation of dual-specificity phosphatase MKP3 by extracellular regulated kinase, D. Rigas, R.H. Hoff, A.E. Rice, A.C. Hengge and J.M. Denu. Biochemistry. 2001, 40, 4398-4406.

The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: a computational and isotope effect study, P.G. Czyryca and A.C. Hengge. Biochim. Biophys. Acta, 2001, 1547, 245-53.

Isotope effects in the study of enzymatic phosphoryl transfer reactions, A.C. Hengge. FEBS Letters. 2001, 501, 99-102. (Invited review)

Isotope Effects and Medium Effects on Sulfuryl Transfer Reactions, R.H. Hoff, P. Larsen and A. C. Hengge. J. Am. Chem. Soc. 2001, 123, 9338-9344.

Mutation of Arg-166 of Alkaline Phosphatase Alters the Thio Effect but Not the Transition State for Phosphoryl Transfer. Implications for the Interpretation of Thio Effects in Reactions of Phosphatases, K.M. Holtz, I.E. Catrina, A.C. Hengge and E.R. Kantrowitz. Biochemistry, 2000, 39, 9451-9458.

Effects on General Acid Catalysis from Mutations of the Invariant Tryptophan and Arginine Residues in the Protein Tyrosine Phosphatase from Yersinia, R.H. Hoff, A.C. Hengge, L. Wu, Y.-F. Keng and Z.-Y. Zhang. Biochemistry, 2000, 39, 46­54.

Kinetic isotope effects and stereochemical studies on a ribonuclease model: Hydrolysis reactions of uridine 3'-nitrophenyl phosphate, A.C. Hengge, K.S. Bruzik, A.E. Tobin, W.W. Cleland and M. D. Tsai. Bioorg. Chem. 2000, 28, 119-133.

Does Positive Charge at the Active Sites of Phosphatases Cause a Change in Mechanism? The Effect of the Conserved Arginine on the Transition State for Phosphoryl Transfer In the Protein-tyrosine Phosphatase from Yersinia, R.H. Hoff, L. Wu, B. Zhou, Z.-Y. Zhang and A.C. Hengge. J. Am. Chem. Soc. 1999, 121, 9514-9521.

Comparison of the Reaction Progress of Calcineurin with Mn²⁺ and Mg²⁺, B.L. Martin, L.A. Jurado and A.C. Hengge. Biochemistry. 1999, 38, 3386-3392.

Comparisons of Phosphorothioate and Phosphate Monoester Transfer Reactions: Activation Parameters, Solvent Effects, and the Effect of Metal Ions, I.E. Catrina and A.C. Hengge. J. Am. Chem. Soc. 1999, 121, 2156-2163.

Insights from Heavy-Atom Isotope Effects on Phosphoryl and Thiophosphoryl Transfer Reactions, A.C. Hengge. In: Enzymatic Mechanisms (Frey, P. A. and Northrop, D. B., Eds.), IOS Press, Amsterdam, 1999. pp. 72-84.

Transfer of the Phosphoryl Group, A.C. Hengge. In: Comprehensive Biological Catalysis: A Mechanistic Reference (Michael Sinnott, Ed.), Academic Press: San Diego, CA, 1998. Vol. 1, Chapter 14, pp 517-542.

A Facile High-Yield Synthesis and Purification of Tetrabutylammonium Tetrabutylborate, R. H. Hoff and A.C. Hengge. J. Org. Chem. 1998, 63, 195.

Isotope Effects on Enzyme-Catalyzed Acyl Transfer from p-Nitrophenyl Acetate: Concerted Mechanisms and Increased Hyperconjugation in the Transition State, R. A. Hess, A.C. Hengge and W.W. Cleland. J. Am. Chem. Soc. 1998, 120, 2703-2709.

Entropy and Enthalpy Contributions to Solvent Effects on Phosphate Monoester Solvolysis. The Importance of Entropy Effects in the Dissociative Transition State, R.H. Hoff and A.C. Hengge. J. Org. Chem. 1998, 63, 6680-6688.

Heavy-Atom Isotope Effects on Reactions of Co(III)-Bound p-Nitrophenyl Phosphate: Nucleophilic Displacements of p-Nitrophenol and Dissociation of p-Nitrophenyl Phosphate, J. Rawlings, A.C. Hengge and W.W. Cleland. J. Am. Chem. Soc. 1997, 119, 542-549.

O-18 Isotope Effects Support a Concerted Mechanism for Ribonuclease A, G.A. Sowa, A.C. Hengge and W.W. Cleland. J. Am. Chem. Soc. 1997, 119, 2319-2320.

Examination of the Transition State of the Low-Molecular Mass Small Tyrosine Phosphatase 1. Comparisons with Other Protein Phosphatases, A.C. Hengge, Y. Zhao, L. Wu, Z.-Y. Zhang. Biochemistry. 1997, 36, 7928-7936.

Isotope Effect Studies on the Calcineurin Phosphoryl-Transfer Reaction: Transition State Structure and Effect of Calmodulin and Mn²⁺, A.C. Hengge and B.L. Martin. Biochemistry. 1997, 36, 10185-10191.

Kinetic Isotope Effects for Acyl Transfer from p-Nitrophenyl Acetate to Hydroxylamine Show a pH-Dependent Change in Mechanism, R.A. Hess, A.C. Hengge, W.W. Cleland. J. Am. Chem. Soc. 1997, 119, 6980-6983.

Characterization of Transition States in Dichloro (1,4,7-Triazacyclononane) Copper(II)-Catalyzed Activated Phosphate Diester Hydrolysis, K.A. Deal, A.C. Hengge and J.N. Burstyn. J. Am. Chem. Soc. 1996, 118, 1713-1718.

Transition-State Structures for the Native Dual-Specific Phosphatase VHR and its D92N and S131A Mutants. Contributions to the Driving Force for Catalysis, A.C. Hengge, J.M. Denu and J.E. Dixon. Biochemistry. 1996, 35, 7084-7092.

The Nature of the Transition State of the Protein-Tyrosine Phosphatase-Catalyzed Reaction, A.C. Hengge, G.A. Sowa, L. Wu and Z.-Y. Zhang. Biochemistry. 1995, 34, 13982-13987.

Mechanisms of Phosphoryl and Acyl Transfer, W.W. Cleland and A.C. Hengge. FASEB Journal. 1995, 9, 1585-1594. (Review article).