Alvan Hengge

Publications | Abstracts

• Anderson, S.N, Nziko, Vincent de Paul Nzuwah, , Chang, C.T, Hengge, A.C, (2014). Enhancing safety in academic research laboratories: Creating a student based safety committee. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Whittier, S., Hengge, A.C, Loria, J.P, (2013). Coupling of Loop Closure and Chemistry in Protein Tyrosine Phosphatases. BIOPHYSICAL JOURNAL *
• Chu, Y., Hengge, A.C, Williams, N.H, (2012). A Simple Arg to Lys Mutant of Protein Phosphatase 1 Exhibits CatalyticEfficiencies toward Monoanionic Substrates Superior to Wild Type. FASEB JOURNAL *
• Kuznetsov, V.I, Johnson, S.J, Hengge, A.C, (2012). High resolution structure of the phosphatase VHZ explains unexpectedsubstrate specificity, and suggests the presence of metavanadate at theactive site. FASEB JOURNAL *
• Haney, M.P, Hengge, A.C, (2012). The phosphoramidase competency of prototypical phosphatase motifs. FASEB JOURNAL *
• Smith, G.K, Ke, Z., Hengge, A.C, Xu, D., Xie, D., Guo, H., (2010). Active-site dynamics of the SpvC virulence factor from Salmonellatyphimurium and density functional model for the catalytic mechanism ofthe phosphthreonine lyase. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Chu, Y., Williams, N.H, Hengge, A.C, (2010). Mechanistic study of phosphoryl transfer reactions catalyzed by proteinphosphatase-1. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Huefner, S.A, Brandao, T.A, Johnson, S.J, Hengge, A.C, (2008). CHED 176-Protein-tyrosine phosphatases: Comparing the effects ofmutation on protein conformation and catalysis. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Brandao, T.A, Huefner, S.A, Johnson, S.J, Hengge, A.C, (2008). BIOL 97-Protein conformational changes in catalysis by protein-tyrosinephosphatases. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Tanifum, E.A, Hengge, A.C, Lund, E.A, Williams, N.H, Feng, G., McWhirter, C., (2007). ORGN 724-Comparative mechanistic studies on the catalyticallypromiscuous serine/threonine protein phosphatase-1 (PP-1) and thedinuclear cobalt(III) complex [Co2(tacn)2(OH)3](ClO4)3. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Iyer, S., Hengge, A.C, (2007). Effect of thio-substitution on the mechanisms of transesterification ofribonucleoside phosphodiester models. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Sorensen-Stowell, K., Hengge, A.C, (2005). Use of O-18 isotope shifts on P-31 NMR to probe potential medium effectson phosphate ester bond strengths.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Humphry, T., Forconi, M., Williams, N., Hengge, A.C, (2003). Alteration of the mechanisms of phosphate ester hydrolysis bycomplexation to a dinuclear metal cneter.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Swierczek, K., Hengge, A.C, (2003). Comparison of phosphonothioic acids with phosphonic acids as inhibitorsof phosphatase.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Purcell, J., Hengge, A.C, (2003). Mechanistic studies of phosphoryl and thiophosphoryl group transfer.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Younker, J., Hengge, A.C, (2003). Mechanistic study of aryl aryl sulfate diesters.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Iyer, S., Younker, J., Czyryca, P., Hengge, A.C, (2003). Synthesis and evaluation of aryloxymethyl and aryloxyethyl phosphonatesas inhibitors of phosphatases.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Hengge, A.C, Catrina, I., (2002). Are phosphorothioates valid mechanistic probes for enzymatic phosphoryltransfer?. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Hengge, A.C, Humphry, T., Forconi, M., Williams, N., (2001). Mechanism of reaction of phosphate esters coordinated to a model ofdinuclear metallophosphatases.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
• Hengge, A.C, Grzyska, P., Czyryca, P., Golightly, J., Small, K., Larsen, P., Hoff, R., (2001). Medium effects on phosphoryl transfer reactions and their possibleapplicability to enzymatic phosphoryl transfer.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Hengge, A.C, Czyryca, P., (2001). Novel motif for the design of transition state analogs for phosphatases.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Hengge, A.C, (2001). Transition states for phosphoryl transfer reactions of phosphatases andtheir application to inhibitor design.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Hengge, A.C, Czyryca, P., (2001). A novel motif for the design of transition state analogues for phosphatases.. BIOCHEMISTRY *
• Hengge, A.C, Humphry, T., Forconi, M., Williams, N., (2001). Mechanism of reaction of phosphate esters coordinated to a model ofdinuclear metallophosphatases.. BIOCHEMISTRY *
• Rawlings, J., Hengge, A.C, Cleland, W., (1999). Cn(III)and Zn(II) catalyzed hydrolysis of phosphodiesters.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Hoff, R., Hengge, A.C, (1998). Entropy effects in the catalytic efficiency of phosphatases. FASEB JOURNAL *
• Catrina, I., Hengge, A.C, (1998). Solution and enzymatic reactions of phosphorothioate monoesters:Thermodynamics and mechanisms. FASEB JOURNAL *
• Hoff, R., Hengge, A.C, (1997). Thermodynamics of solvation effects on phosphoryl and sulfuryl.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Hengge, A.C, Zhang, Z., Denu, J., Dixon, J., (1996). Isotope effect studies of the dual-specific phosphatases VHR and STP1. FASEB JOURNAL *
• RAWLINGS, J., Hengge, A.C, CLELAND, W., (1995). HEAVY-ATOM ISOTOPE EFFECTS ON CO(III)-CATALYZED HYDROLYSIS OFP-NITROPHENYLPHOSPHATE. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY *
• Hengge, A.C, ZHANG, Z., (1995). KINETIC ISOTOPE EFFECTS ON REACTIONS OF TYROSINE PHOSPHATASES. FASEB JOURNAL *
• RAWLINGS, J., Hengge, A.C, CLELAND, W., (1994). ISOTOPE EFFECTS ON THE HYDROLYSIS OF COBALT(III)-BOUND PHOSPHATE-ESTERS. FASEB JOURNAL *

An asterisk (*) at the end of a publication indicates that it has not been peer-reviewed.

Publications | Book Chapters

• Chu, Y., Hengge, A.C, (2010). Phosphatases: Encyclopedia of Catalysis, Second Edition.
• Brandao, T.A, Hengge, A.C, (2010). Phosphoryl and Sulfuryl Transfer: Comprehensive Natural Products II: Chemistry and Biology. Elsevier
• Hengge, A.C, (2005). Mechanistic studies on enzyme-catalyzed phosphoryl transfer: ADVANCES IN PHYSICAL ORGANIC CHEMISTRY, VOL 40.
• Hengge, A.C, (2003). Kinases: Encyclopedia of Catalysis.
• Hengge, A.C, (2003). Phosphatases: Encyclopedia of Catalysis.

An asterisk (*) at the end of a publication indicates that it has not been peer-reviewed.

Publications | Journal Articles

Academic Journal

• Hengge, A.C, Shen, R., Brownless, A.R, Alansson, N., Corbella, M., Kamerlin, S.C, (2024). SHP-1 Variants Broaden the Understanding of pH-Dependent Activities in Protein Tyrosine Phosphatases. JACS Au, 4, 2874-2885.
• Crean, R., Corbella, M., Calixto, A., Hengge, A.C, Kamerlin, L., (2024). Sequence – Dynamics – Function Relationships in Protein Tyrosine Phosphatases. QRB Discovery, doi: https://doi.org/10.1017/qrd.2024.3
• Shen, R., Crean, R.M, Olsen, K.J, Corbella, M., Calixto, A.R, Richan, T., Brandão, T.A, Berry, R.D, Tolman, A., Loria, J.P, Johnson, S.J, Kamerlin, S.C, Hengge, A.C, (2022). Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases. Chem. Sci., 13524-13540. doi: https://doi.org/10.1039/D2SC04135A
• Pinkston, J., Shen, R., Simons, C.R, Hengge, A.C, (2022). Competitive Measurement of β/α Naphthyl Phosphate Catalytic Efficiency by Phosphatases Utilizing Quantitative NMR. Analytical Biochemistry, 651, doi: https://doi.org/10.1016/j.ab.2022.114727
• Crean, R.M, Biler, M., van der Kamp, M.W, Hengge, A.C, Kamerlin, S.C, (2021). Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases. Journal of the American Chemical Society, 143:10, 3830-3845.
• Hengge, A.C, (2021). Plasmodium falciparum finds the winning combination. Journal of Biological Chemistry, 296, 100526.
• Shen, R., Crean, R.M, Johnson, S.J, Kamerlin, S.C, Hengge, A.C, (2021). Single Residue on the WPD-Loop Affects the pH Dependency of Catalysis in Protein Tyrosine Phosphatases. JACS Au, 1:5, 646-659.
• Pinkston, J., Jo, J., Olsen, K.J, Comer, D., Glaittli, C.A, Loria, J.P, Johnson, S.J, Hengge, A.C, (2021). Significant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality. Biochemistry, 60:38, 2888-2901.
• Szeler, K., Williams, N.H, Hengge, A.C, Kamerlin, S.C, (2020). Modeling the Alkaline Hydrolysis of Diaryl Sulfate Diesters: A Mechanistic Study. The Journal of Organic Chemistry, 85:10, 6489-6497.
• Costa, D.M, Gómez, S.V, S. de Araújo, S., Pereira, M.S, Alves, R.B, Favaro, D.C, Hengge, A.C, Nagem, R.A, Brandão, T.A, (2019). Catalytic mechanism for the conversion of salicylate into catechol by the flavin-dependent monooxygenase salicylate hydroxylase. International Journal of Biological Macromolecules, 129, 588-600.
• Bigley, A.N, Xiang, D.F, Narindoshvili, T., Burgert, C.W, Hengge, A.C, Raushel, F.M, (2019). Transition State Analysis of the Reaction Catalyzed by the Phosphotriesterase from Sphingobium sp. TCM1. Biochemistry, 58:9, 1246-1259.
• van Loo, B., Berry, R., Boonyuen, U., Mohamed, M.F, Golicnik, M., Hengge, A.C, Hollfelder, F., (2019). Transition-State Interactions in a Promiscuous Enzyme: Sulfate and Phosphate Monoester Hydrolysis by Pseudomonas aeruginosa Arylsulfatase. Biochemistry, 58:10, 1363-1378.
• Moise, G., Morales, Y., Beaumont, V., Caradonna, T., Loria, J.P, Johnson, S.J, Hengge, A.C, (2018). A YopH PTP1B Chimera Shows the Importance of the WPD-Loop Sequence to the Activity, Structure, and Dynamics of Protein Tyrosine Phosphatases. Biochemistry, 57:36, 5315-5326.
• Chu, Y., Williams, N.H, Hengge, A.C, (2017). Transition States and Control of Substrate Preference in the Promiscuous Phosphatase PP1. Biochemistry, 56:30, 3923-3933. doi: 10.1021/acs.biochem.7b00441
• Pereira, M.S, Murta, B., Oliveira, T.C, Manfredi, A.M, Nome, F., Hengge, A.C, Brandao, T.A, (2016). Mechanistic Aspects of Phosphate Diester Cleavage Assisted by Imidazole.A Template Reaction for Obtaining Aryl Phosphoimidazoles. Journal of Organic Chemistry, 81:19, 8663-8672.
• Coitinho, J.B, Pereira, M.S, Costa, D.M, Guimaraes, S.L, Araujo, S.S, Hengge, A.C, Brandao, T.A, Nagem, R.A, (2016). Structural and Kinetic Properties of the Aldehyde Dehydrogenase NahF, aBroad Substrate Specificity Enzyme for Aldehyde Oxidation. Biochemistry, 55:38, 5453-5463. doi: 10.1021/acs.biochem.6b00614
• Hengge, A.C, (2015). Kinetic Isotope Effects In The Characterization Of Catalysis by Protein Tyrosine Phosphatases. Biochemica et Biophysica Acta - Proteins and Proteomics , 1854, 1768-1775. doi: 10.1016/j.bbapap.2015.03.010
• Moise, G., Gallup, N.M, Alexandrova, .N, Hengge, A.C, Johnson, S.J, (2015). Conservative Tryptophan Mutants of the Protein Tyrosine Phosphatase YopH Exhibit Impaired WPD-Loop Function and Crystallize with Divanadate Esters in Their Active Sites. Biochemistry, 54:42, 6490-6500. doi: 10.1021/acs.biochem.5b00496
• Whittier, S.K, Hengge, A.C, Loria, J.P, (2013). Conformational Motions Regulate Phosphoryl Transfer in Related Protein Tyrosine Phosphatases. Science, 341, 899-903. doi: 10.1126/science.1241735
• Kuznetsov, V.I, Hengge, A.C, (2013). New Functional Aspects of the Atypical Protein Tyrosine Phosphatase VHZ. Biochemistry, 52:45, 8012-8025. doi: 10.1021/bi400776z
• Hengge, A.C, (2013). Chemistry and mechanism of phosphatases, diesterases and triesterases. Biochimica et Biophysica Acta, 1834:1, 415-416. doi: 10.1016/j.bbapap.2012.09.013
• Hengge, A.C, Kuznetsov, V.I, Alexandrova, A.N, (2012). Metavanadate at the Active Site of the Phosphatase VHZ. Journal of the American Chemical Society, 134:35, 14298-14301. doi: 10.1021/ja305579h
• Kuznetsov, V.I, Hengge, A.C, Johnson, S.J, (2012). New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening. Biochemistry, 51:49, 9869-9879. doi: 10.1021/bi300908y
• Brandao, T.A, Johnson, S.J, Hengge, A.C, (2012). The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B. Archives of Biochemistry and Biophysics, 525:1, 53-59. doi: doi.org/10.1016/j.abb.2012.06.002
• Smith, G.K, Ke, Z., H.G, Hengge, A.C, (2011). Insights into the Phosphoryl Transfer Mechanism of Cyclin-Dependent Protein Kinases from ab Initio QM/MM Free-Energy Studies. Journal of Physical Chemistry B, 115:46, 13713-13722.
• Mitic, N., Hadler, K.S, Gahan, L.R, Hengge, A.C, Schenk, G., (2010). The Divalent Metal Ion in the Active Site of Uteroferrin Modulates Substrate Binding and Catalysis. Journal of the American Chemical Society, 132:20, 7049-7054. doi: 10.1021/ja910583y
• Brandao, T.A, Hengge, A.C, Johnson, S.J, (2010). Insights into the reaction of protein tyrosine phosphatase 1B. Crystal structures for transition-state analogs of both catalytic steps. Journal of Biological Chemistry, 285:21, 15874-15883. doi: 10.1074/jbc.M109.066951
• Smith, G.K, Ke, Z., Hengge, A.C, Xu, D., Xie, D., Guo, H., (2009). Active-Site Dynamics of SpvC Virulence Factor from Salmonella typhimurium and Density Functional Theory Study of Phosphothreonine Lyase Catalysis. Journal of Physical Chemistry B, 113:46, 15327-15333. doi: 10.1021/jp9052677
• Brandao, T.A, Robinson, H., Johnson, S.J, Hengge, A.C, (2009). Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures. Journal of the American Chemical Society, 131:2, 778-786.
• Feng, G., Tanifum, E.A, Adams, H., Hengge, A.C, Williams, N.H, (2009). Mechanism and Transition State Structure of Aryl Methylphosphonate Esters Doubly Coordinated to a Dinuclear Cobalt(III) Center. Journal of the American Chemistry Society, 131:35, 12771-12779. doi: 10.1021/ja904134n
• Humphry, T., Iyer, S., Iranzo, O., Morrow, J.R, Richard, J.P, Paneth, P., Hengge, A.C, (2008). Altered Transition State for the Reaction of an RNA Model Catalyzed by aDinuclear Zinc(II) Catalyst. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 130:52, 17858-17866.
• Humphry, T., Iyer, S., Iranzo, O., Morrow, J.R, Richard, J.P, Paneth, P., Hengge, A.C, (2008). An Altered Transition State for the Reaction of an RNA Model Catalyzed by a Dinuclear Zinc(II) Catalyst. Journal of the American Chemistry Society, 130:52, 17858-17866.
• McWhirter, C., Lund, E.A, Tanifum, E.A, Feng, G., Sheikh, Q.L, Hengge, A.C, Williams, N.H, (2008). Mechanistic Study of Protein Phosphatase-1 (PP1), A Catalytically Promiscuous Enzyme. Journal of the American Chemistry Society, 130:41, 13673-13682.
• Hadler, K.S, Tanifum, E.A, Yip, S.H, Mitic, N., Guddat, L.W, Jackson, C.J, Gahan, L.R, Nguyen, K., Carr, P.D, Ollis, D.L, Hengge, A.C, Larrabee, J.A, Schenk, G., (2008). Substrate-Promoted Formation of a Catalytically Competent Binuclear Center and Regulation of Reactivity in a Glycerophosphodiesterase from Enterobacter aerogenes. Journal of the American Chemistry Society, 130:41, 14129-14138.
• Iyer, S., Hengge, A.C, (2008). The Effects of Sulfur Substitution for the Nucleophile and Bridging Oxygen Atoms in Reactions of Hydroxyalkyl Phosphate Esters. Journal of Organic Chemistry, 73:13, 4819-4829.
• Brandao, T.A, Robinson, H., Johnson, S.J, Hengge, A.C, (2008). Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures. Journal of the American Chemical Society, 131:2, 778-786. doi: 10.1021/ja807418b
• Cox, R.S, Schenk, G., Mitic, N., Gahan, L., Hengge, A.C, (2007). Diesterase Activity and Substrate Binding in Purple Acid Phosphatases. J. Am. Chem. Soc., 129:31, 9550-9551.
• Zalatan, J.G, Catrina, I., Mitchell, R., Grzyska, P.K, O'Brien, P.J, Herschlag, D., Hengge, A.C, (2007). Kinetic Isotope Effects for Alkaline Phosphatase Reactions: Implications for the Role of Active-Site Metal Ions in Catalysis. J. Am. Chem. Soc., 129:31, 9789-9796.
• Wong, F.M, Wang, J., Hengge, A.C, Wu, W., (2007). Mechanism of Rhodium-Catalyzed Carbene Formation from Diazo Compounds. Org. Lett., 9:9, 1663-1665.
• Catrina, I., O'Brien, P.J, Purcell, J., Nikolic-Hughes, I., Zalatan, J.G, Hengge, A.C, Herschlag, D., (2007). Probing the Origin of the Compromised Catalysis of E. coli Alkaline Phosphatase in its Promiscuous Sulfatase Reaction. J. Am. Chem. Soc. , 129:17, 5760-5765.
• Hoff, R.H, Hengge, A.C, (2007). The Use of Isotopes in the Study of Reactions of Acyl, Phosphoryl, and Sulfuryl Esters. Journal of Labelled Compounds and Radiopharmaceuticals, 50, 1026-1038.
• Lund, E.A, Hengge, A.C, Williams, N.H, McWhirter, C., Feng, G., (2007). Mechanistic study of PP-1, a catalytically promiscuous enzyme. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 233, 613.
• Rawlings, J., Cleland, W.W, Hengge, A.C, (2006). Metal-catalyzed phosphodiester cleavage: Secondary O-18 isotope effectsas an indicator of mechanism. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 128:51, 17120-17125.
• Hoff, R.H, Czyryca, P.G, Sun, M., Leyh, T.S, Hengge, A.C, (2006). Transition state of the sulfuryl transfer reaction of estrogensulfotransferase. JOURNAL OF BIOLOGICAL CHEMISTRY, 281:41, 30645-30649.
• Sorensen-Stowell, K., Hengge, A.C, (2006). Thermodynamic origin of the increased rate of hydrolysis of phosphateand phosphorothioate esters in DMSO/water mixtures. JOURNAL OF ORGANIC CHEMISTRY, 71:19, 7180-7184.
• Cleland, W.W, Hengge, A.C, (2006). Enzymatic mechanisms of phosphate and sulfate transfer. CHEMICAL REVIEWS, 106:8, 3252-3278.
• Liu, Y., Gregersen, B.A, Hengge, A.C, York, D.M, (2006). Transesterification thio effects of phosphate diesters: Free energybarriers and kinetic and equilibrium isotope effects fromdensity-functional theory. BIOCHEMISTRY, 45:33, 10043-10053.
• Sorensen-Stowell, K., Hengge, A.C, (2005). Probing potential medium effects on phosphate ester bonds using O-18isotope shifts on P-31 NMR. JOURNAL OF ORGANIC CHEMISTRY, 70:21, 8303-8308.
• Purcell, J., Hengge, A.C, (2005). Thermodynamics of phosphate versus phosphorothioate ester hydrolysis. JOURNAL OF ORGANIC CHEMISTRY, 70:21, 8437-8442.
• Onyido, I., Swierczek, K., Purcell, J., Hengge, A.C, (2005). A concerted mechanism for the transfer of the thiophosphinoyl group fromaryl dimethylphosphinothioate esters to oxyanionic nucleophiles inaqueous solution. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 127:21, 7703-7711.
• Sorensen-Stowell, K., Hengge, A.C, (2005). Examination of P-OR bridging bond orders in phosphate monoesters usingO-18 isotope shifts in P-31 NMR. JOURNAL OF ORGANIC CHEMISTRY, 70:12, 4805-4809.
• Hengge, A.C, Onyido, I., (2005). Physical organic perspectives on phospho group transfer from phosphatesand phosphinates. CURRENT ORGANIC CHEMISTRY, 9:1, 61-74.
• Younker, J., Hengge, A.C, (2004). A mechanistic study of the alkaline hydrolysis of diaryl sulfatediesters. JOURNAL OF ORGANIC CHEMISTRY, 69:26, 9043-9048.
• Iyer, S., Younker, J., Czyryca, P., Hengge, A.C, (2004). A nohydrolyzale analogue of phosphotyrosine, and related aryloxymethano-and aryloxyethano-phosponic acids as motifs for inhibition ofphosphatases. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 14:23, 5931-5935.
• Humphry, T., Forconi, M., Williams, N., Hengge, A.C, (2004). Altered mechanisms of reactions of phosphate esters bridging a dinuclearmetal center. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 126:38, 11864-11869.
• Grzyska, P., Kim, Y., Jackson, M., Hengge, A.C, Denu, J., (2004). Probing the transition-state structure of dual-specificity proteinphosphatases using a physiological substrate mimic. BIOCHEMISTRY, 43:27, 8807-8814.
• Gibby, S., Younker, J., Hengge, A.C, (2004). Investigation of the sulfuryl transfer step from substrate to enzyme byarylsulfatases. JOURNAL OF PHYSICAL ORGANIC CHEMISTRY, 17:6-7, 541-547.
• McCain, D., Grzyska, P., Wu, L., Hengge, A.C, Zhang, Z., (2004). Mechanistic studies of protein tyrosine phosphatases YopH and Cdc25Awith m-nitrobenzyl phosphate. BIOCHEMISTRY, 43:25, 8256-8264.
• Hengge, A.C, Stein, R., (2004). Role of protein conformational mobility in enzyme catalysis: Acylationof alpha-chymotrypsin by specific peptide substrates. BIOCHEMISTRY, 43:3, 742-747.
• Grzyska, P., Czyryca, P., Purcell, J., Hengge, A.C, (2003). Transition state differences in hydrolysis reactions of alkyl versusaryl phosphate monoester monoanions. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 125:43, 13106-13111.
• Swierczek, K., Pandey, A., Peters, J., Hengge, A.C, (2003). A comparison of phosphonothioic acids with phosphonic acids asphosphatase inhibitors. JOURNAL OF MEDICINAL CHEMISTRY, 46:17, 3703-3708.
• Iyer, S., Younker, J., Czyryca, P., Hengge, A.C, (2003). Synthesis and evaluation of aryloxymethyl and aryloxyethyl phosphonatesas inhibitors of phosphatases.. BIOCHEMISTRY, 42:28, 8600-8601.
• Catrina, I., Hengge, A.C, (2003). Comparisons of phosphorothioate with phosphate transfer reactions for amonoester, diester, and triester: Isotope effect studies. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 125:25, 7546-7552.
• Swierczek, K., Peters, J., Hengge, A.C, (2003). A convenient synthesis of phosphonothioic acids. TETRAHEDRON, 59:5, 595-599.
• Rawlings, J., Cleland, W., Hengge, A.C, (2003). Metal ion catalyzed hydrolysis of ethyl p-nitrophenyl phosphate. JOURNAL OF INORGANIC BIOCHEMISTRY, 93:1-2, 61-65.
• Humphry, T., Forconi, M., Williams, N., Hengge, A.C, (2002). An altered mechanism of hydrolysis for a metal-complexed phosphatediester. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 124:50, 14860-14861.
• Catrina, I., Czyryca, P., Hengge, A.C, (2002). Isotope effects on enzymatic and nonenzymatic reactions ofphosphorothioates. NUKLEONIKA, 47:1, S17-S23.
• McCain, D., Catrina, I., Hengge, A.C, Zhang, Z., (2002). The catalytic mechanism of Cdc25A phosphatase. JOURNAL OF BIOLOGICAL CHEMISTRY, 277:13, 11190-11200.
• Grzyska, P., Czyryca, P., Golightly, J., Small, K., Larsen, P., Hoff, R., Hengge, A.C, (2002). Generality of solvation effects on the hydrolysis rates of phosphatemonoesters and their possible relevance to enzymatic catalysis. JOURNAL OF ORGANIC CHEMISTRY, 67:4, 1214-1220.
• Hengge, A.C, (2002). Isotope effects in the study of phosphoryl and sulfuryl transferreactions. ACCOUNTS OF CHEMICAL RESEARCH, 35:2, 105-112.
• Hoff, R., Larsen, P., Hengge, A.C, (2001). Isotope effects and medium effects on sulfuryl transfer reactions. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 123:38, 9338-9344.
• Hengge, A.C, (2001). Isotope effects in the study of enzymatic phosphoryl transfer reactions. FEBS LETTERS, 501:2-3, 99-102.
• Hengge, A.C, Grzyska, P., Czyryca, P., Golightly, J., Small, K., Larsen, P., Hoff, R., (2001). Medium effects on phosphoryl transfer reactions and their possibleapplicability to enzymatic phosphoryl transfer.. BIOCHEMISTRY, 40:29, 8622-8623.
• Czyryca, P., Hengge, A.C, (2001). The mechanism of the phosphoryl transfer catalyzed by Yersiniaprotein-tyrosine phosphatase: a computational and isotope effect study. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1547:2, 245-253.
• Rigas, J., Hoff, R., Rice, A., Hengge, A.C, Denu, J., (2001). Transition state analysis and requirement of Asp-262 general acid/basecatalyst for full activation of dual-specificity phosphatase MKP3 byextracellular regulated kinase. BIOCHEMISTRY, 40:14, 4398-4406.
• Rishavy, M., Hengge, A.C, Cleland, W., (2000). Lanthanide catalyzed cyclization of uridine 3 ‘-p-nitrophenyl phosphate. BIOORGANIC CHEMISTRY, 28:5, 283-292.
• Holtz, K., Catrina, I., Hengge, A.C, Kantrowitz, E., (2000). Mutation of Arg-166 of alkaline phosphatase alters the thio effect butnot the transition state for phosphoryl transfer. Implications for theinterpretation of thio effects in reactions of phosphatases. BIOCHEMISTRY, 39:31, 9451-9458.
• Hengge, A.C, Bruzik, K., Tobin, A., Cleland, W., Tsai, M., (2000). Kinetic isotope effects and stereochemical studies on a ribonucleasemodel: Hydrolysis reactions of uridine 3 ‘-nitrophenyl phosphate. BIOORGANIC CHEMISTRY, 28:3, 119-133.
• Hoff, R., Hengge, A.C, Wu, L., Keng, Y., Zhang, Z., (2000). Effects on general acid catalysis from mutations of the invarianttryptophan and arginine residues in the protein tyrosine phosphatasefrom Yersinia. BIOCHEMISTRY, 39:1, 46-54.
• Hoff, R., Wu, L., Zhou, B., Zhang, Z., Hengge, A.C, (1999). Does positive charge at the active sites of phosphatases cause a changein mechanism? The effect of the conserved arginine on the transitionstate for phosphoryl transfer in the protein-tyrosine phosphatase fromYersinia. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 121:41, 9514-9521.
• Hoff, R., Mertz, P., Rusnak, F., Hengge, A.C, (1999). The transition state of the phosphoryl-transfer reaction catalyzed bythe lambda Ser/Thr protein phosphatase. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 121:27, 6382-6390.
• Martin, B., Jurado, L., Hengge, A.C, (1999). Comparison of the reaction progress of calcineurin with Mn2+ and Mg2+. BIOCHEMISTRY, 38:11, 3386-3392.
• Catrina, I., Hengge, A.C, (1999). Comparisons of phosphorothioate and phosphate monoester transferreactions: Activation parameters, solvent effects, and the effect ofmetal ions. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 121:10, 2156-2163.
• Hoff, R., Hengge, A.C, (1998). Entropy and enthalpy contributions to solvent effects on phosphatemonoester solvolysis. The importance of entropy effects in thedissociative transition state. JOURNAL OF ORGANIC CHEMISTRY, 63:19, 6680-6688.
• Hess, R., Hengge, A.C, Cleland, W., (1998). Isotope effects on enzyme-catalyzed acyl transfer from p-nitrophenylacetate: Concerted mechanisms and increased hyperconjugation in thetransition state. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 120:12, 2703-2709.
• Hoff, R., Hengge, A.C, (1998). A facile high-yield synthesis and purification of tetrabutylammoniumtetrabutylborate. JOURNAL OF ORGANIC CHEMISTRY, 63:1, 195.
• Hengge, A., Martin, B., (1997). Isotope effect studies on the calcineurin phosphoryl-transfer reaction:Transition state structure and effect of calmodulin and Mn2+. BIOCHEMISTRY, 36:33, 10185-10191.
• Hess, R., Hengge, A., Cleland, W., (1997). Kinetic isotope effects for acyl transfer from p-nitrophenyl acetate tohydroxylamine show a pH-dependent change in mechanism. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 119:30, 6980-6983.
• Hengge, A., Zhao, Y., Wu, L., Zhang, Z., (1997). Examination of the transition state of the low-molecular mass smalltyrosine phosphatase .1. Comparisons with other protein phosphatases. BIOCHEMISTRY, 36:25, 7928-7936.
• Sowa, G., Hengge, A., Cleland, W., (1997). O-18 isotope effects support a concerted mechanism for ribonuclease A. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 119:9, 2319-2320.
• Rawlings, J., Hengge, A., Cleland, W., (1997). Heavy-atom isotope effects on reactions of Co(III)-bound p-nitrophenylphosphate: Nucleophilic displacements of p-nitrophenol and dissociationof p-nitrophenyl phosphate. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 119:3, 542-549.
• Hengge, A., Denu, J., Dixon, J., (1996). Transition-state structures for the native dual-specific phosphatase VHRand D92N and S131A mutants, contributions to the driving force forcatalysis. BIOCHEMISTRY, 35:22, 7084-7092.
• Deal, K., Hengge, A.C, Burstyn, J., (1996). Characterization of transition states indichloro(1,4,7-triazacyclononane)copper(II)-catalyzed activatedphosphate diester hydrolysis. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 118:7, 1713-1718.
• Cleland, W., Hengge, A., (1995). Mechanisms of phosphoryl and acyl transfer. FASEB JOURNAL, 9:15, 1585-1594.
• Hengge, A.C, SOWA, G., WU, L., ZHANG, Z., (1995). NATURE OF THE TRANSITION-STATE OF THE PROTEIN-TYROSINEPHOSPHATASE-CATALYZED REACTION. BIOCHEMISTRY, 34:43, 13982-13987.
• Hengge, A.C, TOBIN, A., CLELAND, W., (1995). STUDIES OF TRANSITION-STATE STRUCTURES IN PHOSPHORYL TRANSFER-REACTIONSOF PHOSPHODIESTERS OF P-NITROPHENOL. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 117:22, 5919-5926.
• Hengge, A.C, HESS, R., (1994). CONCERTED OR STEPWISE MECHANISMS FOR ACYL TRANSFER-REACTIONS OFP-NITROPHENYL ACETATE - TRANSITION-STATE STRUCTURES FROM ISOTOPE EFFECTS. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 116:25, 11256-11263.
• Hengge, A.C, EDENS, W., ELSING, H., (1994). TRANSITION-STATE STRUCTURES FOR PHOSPHORYL-TRANSFER REACTIONS OFP-NITROPHENYL PHOSPHATE. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 116:12, 5045-5049.
• Hengge, A.C, (1992). CAN ACYL TRANSFER OCCUR VIA A CONCERTED MECHANISM - DIRECT EVIDENCE FROMHEAVY-ATOM ISOTOPE EFFECTS. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 114:16, 6575-6576.
• Hengge, A.C, (1992). O-18 EXCHANGE IN NITROPHENOLS - SIGNIFICANCE FOR LABELING AND ISOTOPEEFFECT EXPERIMENTS. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 114:7, 2747-2748.
• WILSON, R., Hengge, A.C, ATAEI, A., HO, D., (1991). OXIDATIVE-ALPHA COUPLING OF CARBONYL-COMPOUNDS VIA THE CONDENSATION OFACYLATED TRIAZOLINEDIONE YLIDES WITH ENOLATES - A FACILE SYNTHESIS OFPOLYACYLATED OLEFINS. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 113:19, 7240-7249.
• Hengge, A.C, CLELAND, W., (1991). PHOSPHORYL-TRANSFER REACTIONS OF PHOSPHODIESTERS - CHARACTERIZATION OFTRANSITION-STATES BY HEAVY-ATOM ISOTOPE EFFECTS. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 113:15, 5835-5841.
• Hengge, A.C, CLELAND, W., (1991). MECHANISM OF PHOSPHODIESTER CLEAVAGE WITH BETA-CYCLODEXTRIN. JOURNAL OF ORGANIC CHEMISTRY, 56:5, 1972-1974.
• Hengge, A.C, CLELAND, W., (1990). DIRECT MEASUREMENT OF TRANSITION-STATE BOND-CLEAVAGE IN HYDROLYSIS OFPHOSPHATE-ESTERS OF P-NITROPHENOL. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 112:20, 7421-7422.
• WILSON, R., Hengge, A.C, ATAEI, A., CHANTARASIRI, N., (1990). ADDITION OF 4-PHENYLTRIAZOLINEDIONE TO CARBONYL-COMPOUNDS - THEFORMATION OF ALPHA-URAZOLYLCARBONYL COMPOUNDS. JOURNAL OF ORGANIC CHEMISTRY, 55:1, 193-197.
• WILSON, R., Hengge, A.C, (1990). SYNTHESIS AND CHEMISTRY OF ACYLTRIAZOLINEDIONE YLIDES AND RELATEDINTERMEDIATES - NEW METHODS FOR THE PREPARATION OF DICARBONYL ANDTRICARBONYL COMPOUNDS. JOURNAL OF ORGANIC CHEMISTRY, 55:1, 197-202.
• WILSON, R., Hengge, A.C, (1987). NUCLEOPHILIC ADDITIONS TO TRIAZOLINEDIONE YLIDES, EXTREMELY REACTIVECARBONYL EQUIVALENTS - A NEW CLASS OF CONDENSATION-REACTIONS. JOURNAL OF ORGANIC CHEMISTRY, 52:13, 2699-2707.
• WILSON, R., Hengge, A.C, (1985). THE CHEMISTRY OF AN AZOMETHINE IMINE DERIVED FROM 2,3-DIMETHYLINDOLE ANDN-PHENYL TRIAZOLINEDIONE - A NEW AND FACILE CONDENSATION METHOD. TETRAHEDRON LETTERS, 26:31, 3673-3676.

An asterisk (*) at the end of a publication indicates that it has not been peer-reviewed.

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Other

• Hengge, A.C, (2008). NMR data do not implicate a phosphorane in the T4 DNA ligase reaction. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OFAMERICA *

An asterisk (*) at the end of a publication indicates that it has not been peer-reviewed.