:: Publications in last 5 years (for a full list of references, click here)

The Divalent Metal Ion in the Active Site of Uteroferrin Modulates Substrate Binding and Catalysis. Natasa Mitic, Kieran S. Hadler, Lawrence R. Gahan, Alvan C. Hengge and Gerhard Schenk, J. Am. Chem. Soc. 2010, 132 (20), 7049–7054.

Insights into the Reaction of Protein-tyrosine Phosphatase 1B: Crystal Structures for Transition State Analogs of Both Catalytic Steps. Tiago A. S. Brandao, Alvan C. Hengge, and Sean J. Johnson, .”  J. Biol. Chem. 2010, 285 (21), 15874-15883. 

Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures. Tiago A. S. Brandão, H. Robinson, S. J. Johnson,and A. C. Hengge, J. Am. Chem. Soc. 2009, 131 (2), 778-786.

Active-Site Dynamics of SpvC Virulence Factor from Salmonella typhimurium and Density Functional Theory Study of Phosphothreonine Lyase Catalysis, G. K. Smith, Z. Ke, A. C. Hengge, D. Xu, D. Xie and H. Guo,  J. Phys. Chem. B, 2009, 113, 15327–15333.

Mechanism and Transition State Structure of Aryl Methylphosphonate Esters Doubly Coordinated to a Dinuclear Cobalt(III) Center, G. Feng, E. A. Tanifum, H. Adams, A. C. Hengge and N. H. Williams, . Am. Chem. Soc. 2009, 131, 12771-12779.

Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures, T. A. S. Brandão, H. Robinson, S. J. Johnson, and A. C. Hengge, J. Am. Chem. Soc., 2008, in press.

Mechanistic Study of Protein Phosphatase-1 (PP1), A Catalytically Promiscuous Enzyme,C. McWhirter, E. A. Lund, E. A. Tanifum, G. Feng, Q. L. Sheikh, A. C. Hengge, and N. H. Williams, J. Am. Chem. Soc., 2008, 130, 13673-13682.

Substrate-Promoted Formation of a Catalytically Competent Binuclear Center and Regulation of Reactivity in a Glycerophosphodiesterase from Enterobacter aerogenes, K. S. Hadler, E. A. Tanifum, S. H.-C. Yip, N. Miti_, L. W. Guddat, C. J. Jackson, L. R. Gahan, K. Nguyen, P. D. Carr, D. L. Ollis, A. C. Hengge, J. A. Larrabee, G. Schenk. J. Am. Chem. Soc. 2008, 130, 14129-14138.

An Altered Transition State for the Reaction of an RNA Model Catalyzed by a Dinuclear Zinc(II) Catalyst, T. Humphry, S. Iyer, O. Iranzo, J. R. Morrow, J. P. Richard, Piotr Paneth, and A. C. Hengge, J. Am. Chem. Soc. 2008, 130, 17858-17866.

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.

:: Invited Book Chapters:

Mechanistic Studies on Enzyme-Catalyzed Phosphoryl Transfer. Advances in Physical Organic Chemistry, 2005, 40, 49-108.

Secondary Isotope Effects. In: Isotope Effects in Chemistry and Biology, A. Kohen and H. Limbach (Eds). CRC Press, 2005. Chapter 39, pp. 955-974.