University of Iowa - Daniel M. Quinn

Selected Recent Publications- Daniel M. Quinn

Quinn, D. M. and Sikorski, R. S. “Enzymatic Rate Enhancements” (2007) in Encyclopedia of Life Sciences (www.els.net); Nature Publishing Group, Macmillan Publishers Ltd., London, UK.
Quinn, D. M. “Chapter 41: Theory and Practice of Solvent Isotope Effects” in Isotope Effects in Chemistry and Biology (Kohen, A. and Limbach, H. H., Eds.) CRC Press: Boca Raton, FL, 2006; pp 995-1018.
Tormos, J. R., Wiley, K. L., Seravalli, J., Nachon, F., Masson, P., Nicolet, Y. and Quinn, D. M. “The Reactant State for Substrate-Activated Turnover of Acetylthiocholine by Butyrylcholinesterase is a Tetrahedral Intermediate” J. Am. Chem. Soc. 2005, 127, 14538-14539.
Sikorski, R.S., Malany, S., Seravalli, J. and Quinn, D.M. “Computational Study of Substrate Isotope Effect Probes of Transition State Structure for Acetylcholinesterase Catalysis” Nukleonika 2002, 47, S9-S12.
Quinn, D. M., Feaster, S. R., Nair, H. K., Baker, N. A., Radi_, Z. and Taylor, P. “Delineation and Decomposition of Energies Involved in Quaternary Ammonium Binding in the Active Site of Acetylcholinesterase” J. Am. Chem. Soc. 2000, 122, 2975-2980.
Malany, S., Sawai, M., Sikorski, R. S., Seravalli, J., Quinn, D. M., Radi_, Z., Taylor, P., Velan, B., Kronman, C. and Shafferman, A. “Transition State Structure and Rate Determination for the Acylation Stage of Acetylcholinesterase Catalyzed Hydrolysis of (Acetylthio)choline” J. Am. Chem. Soc. 2000, 122, 2981-2987.
Liang, Y., Medhekar, R., Brockman, H. L., Quinn, D. M. and Hui, D. Y. “Importance of Arginines 63 and 423 in Modulating the Bile Salt-Dependent and Bile Salt-Independent Hydrolytic Activities of Rat Carboxyl Ester Lipase” J. Biol. Chem. 2000, 275, 2404-24046.
Malany, S., Baker, N. VerWeyst, M. Medhekar, R., Quinn, D. M., Velan, B., Kronman, C. and Shafferman, A. “Theoretical and Experimental Investigations of Electrostatic Effects on Acetylcholinesterase Catalysis and Inhibition” Chem. Biol. Interact 1999, 119-120, 99-110.
Quinn, D.M.; Medhekar, R.; Baker, N. (1999) “Chapter 5: Ester Hydrolysis” in Comprehensive Natural Products Chemistry, Vol 5: Enzymes, Enzyme Mechanisms, Proteins, and Aspects of NO Chemistry (Poulter, C.D.; Ed.) Elsevier Science, Oxford, UK, pp 101-137.
Malany, S.; Baker, N. VerWeyst, M. Medhekar, R.; Quinn, D. M.; Velan, B.; Kronman, C.; Shafferman, A. "Theoretical and Experimental Investigations of Electrostatic Effects on Acetylcholinesterase Catalysis and Inhibition" Chem.-Biol. Interact. 1999, 119-120, 99-110.
Malany, S.; Sawai, M.; Sikorski, R. S.; Seravalli, J.; Quinn, D. M.; Radić, Z.; Taylor, P.; Velan, B.; Kronman, C.; Shafferman, A. “Transition State Structure and Rate Determination for the Acylation Stage of Acetylcholinesterase Catalyzed Hydrolysis of (Acetylthio)choline” J. Am. Chem. Soc. 1999, in press.
Medhekar, R.; Baker, N.; Kearney, W.; Sando, K.; Quinn, D.M. “Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Esterases” (1998) in Structure and Function of Cholinesterases and Related Proteins (Doctor, B.P.; Quinn, D.M.; Rotundo, R.; Taylor, P., Eds.) Plenum Press, New York, p 233.
Malany, S.; Sikorski, R. S.; Seravalli, J.; Medhekar, R.; Quinn, D.M.; Radić, Z.; Taylor, P.; Velan, B.; Kronman, C.; Shafferman, A. “Structure of the Acylation Transition State for Acetylcholinesterase Catalysis” (1998) in Structure and Function of Cholinesterases and Related Proteins (Doctor, B.P.; Quinn, D.M.; Rotundo, R. and Taylor, P.; Eds.) Plenum Press, New York, pp 197-202.
Savle, P. S.; Medhekar, R. A.; Kelley, E. L.; May, J. G.; Watkins, S. F.; Fronczek, F. R.; Quinn, D. M.; Gandour, R. D. “Change in the Mode of Inhibition of Acetylcholinesterase by (4-Nitro)benzenesulfonoxy Derivatives of Conformationally Constrained Choline Analogs” Chem. Res. Toxicol. 1998, 11, 19-25.
Quinn, D. M.; Feaster, S. R. “Esterases and Lipases” (1998) in Comprehensive Biological Catalysis (Sinnott, M., Ed.) Vol. 1; Academic Press, London, pp 455-482.
Radić, Z.; Kirchhoff, P.; Quinn, D.M.; McCammon, J.A.; Taylor, P. “Electrostatic Influence on the Kinetics of Ligand Binding to Acetylcholinesterase: Distinctions Between Active Center Ligands and Fasciculin” J. Biol. Chem. 1997, 272, 23265-23277.
Quinn, D.M. “Esterases of the α/β Hydrolase Fold Family” (1997) in Comprehensive Toxicology (Guengerich, F.P., Ed.) Vol. 3: Biotransformation; Elsevier Science, Oxford; pp 243-264.
Saxena, A.; Maxwell, D.M.; Quinn, D.M.; Radić, Z.; Taylor, P.; Doctor, B.P. “Mutant Acetylcholinesterases as Potential Detoxification Agents for Organophosphate Poisoning” Biochem. Pharmacol. 1997, 54, 269-274.
Feaster, S.R.; Quinn, D.M. “Mechanism-Based Inhibitors of Cholesterol Esterase” (1997) in Methods Enzymol. (Rubin, B. and Dennis, E.A.; Eds.) Academic Press, San Diego, pp 231-252.
Feaster, S.R.; Quinn, D.M.; Barnett, B.L. “Molecular Modeling of the Structures of Human and Rat Pancreatic Cholesterol Esterases” Protein Sci. 1997, 6, 71-77.
Feaster, S.R.; Lee, K.; Baker, N.; Hui, D.Y.; Quinn, D.M. “Molecular Recognition by Cholesterol Esterase of Active Site Ligands: Structure-Reactivity Effects for Inhibition by Aryl Carbamates and Subsequent Carbamylenzyme Turnover” Biochemistry 1996, 35, 16723-16734.10.
Hosea, N.A.; Radić, Z.; Tsigelny, I.; Berman, H.A.; Quinn, D.M.; Taylor, P. “Aspartate 74 as a Primary Determinant in Acetylcholinesterase Governing Specificity to Cationic Organophosphonates” Biochemistry 1996, 35 10995-11004.
Harel, M.; Quinn, D.M.; Nair, H.K.; Silman, I.; Sussman, J.L. “The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase” J. Am. Chem. Soc. 1996, 118, 2340-2346.
Radić, Z.; Quinn, D.M.; Vellom, D.C.; Camp, S.; Taylor, P. “Allosteric Control of Acetylcholinesterase Catalysis by Fasciculin” J. Biol. Chem. 1995, 270, 20391-20399.
Quinn, D.M.; Nair, H.K.; Seravalli, J.; Lee, K.; Arbuckle, T.; Radić, Z.; Vellom, D.; Pickering, N.; Taylor, P. “London Dispersion Interactions in Molecular Recognition by Acetylcholinesterase” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd., NewYork and London, pp 228-229.
Quinn, D.M.; Seravalli, J.; Nair, H.K.; Medhekar, R.; Husseini, B.; Radić, Z.; Vellom, D.; Pickering, N.; Taylor, P. “The Function of Electrostatics in Acetylcholinesterase Catalysis” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd.; New York and London, pp 203-207.
Sussman, J.L.; Harel, M.; Raves, M.; Quinn, D.M.; Nair, H.K.; Silman, I. “Structures of Complexes of Acetylcholinesterase with Covalently and Non-covalently Bound Inhibitors” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd., New York and London, pp 59-65.
Ashani, Y.; Doctor, B.P.; Radić, Z.; Vellom, D.C.; Pickering, N.A.; Quinn, D.M.; Taylor, P. “Amino Acid Residues That Control Mono- and Bisquaternary Oxime-induced Reactivation of O-Ethyl Methylphosphonylated Cholinesterases” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd., New York and London, pp 133-140.
Radić, Z.; Quinn, D.M.; Vellom, D.C.; Camp, S.; Taylor, P. “Amino Acid Residues in Acetylcholinesterase Which Influence Fasciculin Inhibition” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd., New York and London, pp 183-188.
Ashani, Y.; Radić, Z.; Tsigelny, I.; Vellom, D.C.; Pickering, N.A.; Quinn, D.M.; Doctor, B.P.; Taylor, P. “Amino Acid Residues Controlling Reactivation of Organophosphonyl Conjugates of Acetylcholinesterase by Mono- and Bisquaternary Oximes” J. Biol. Chem. 1995, 270, 6370-6380.
Sussman, J.L.; Harel, M.; Raves, M.; Quinn, D.; Silman, I. “3-D Structure of Acetylcholinesterase and Its Complexes with Anticholinesterase Agents” (1995) in Modeling of Biomolecular Structures and Mechanisms (A. Pullman et al.; Eds.) Kluwer Academic Publishers, The Netherlands, 455-460.






	Selected Recent Publications- Daniel M. Quinn Quinn, D. M. and Sikorski, R. S. “Enzymatic Rate Enhancements” (2007) in Encyclopedia of Life Sciences (www.els.net); Nature Publishing Group, Macmillan Publishers Ltd., London, UK. Quinn, D. M. “Chapter 41: Theory and Practice of Solvent Isotope Effects” in Isotope Effects in Chemistry and Biology (Kohen, A. and Limbach, H. H., Eds.) CRC Press: Boca Raton, FL, 2006; pp 995-1018. Tormos, J. R., Wiley, K. L., Seravalli, J., Nachon, F., Masson, P., Nicolet, Y. and Quinn, D. M. “The Reactant State for Substrate-Activated Turnover of Acetylthiocholine by Butyrylcholinesterase is a Tetrahedral Intermediate” J. Am. Chem. Soc. 2005, 127, 14538-14539. Sikorski, R.S., Malany, S., Seravalli, J. and Quinn, D.M. “Computational Study of Substrate Isotope Effect Probes of Transition State Structure for Acetylcholinesterase Catalysis” Nukleonika 2002, 47, S9-S12. Quinn, D. M., Feaster, S. R., Nair, H. K., Baker, N. A., Radi_, Z. and Taylor, P. “Delineation and Decomposition of Energies Involved in Quaternary Ammonium Binding in the Active Site of Acetylcholinesterase” J. Am. Chem. Soc. 2000, 122, 2975-2980. Malany, S., Sawai, M., Sikorski, R. S., Seravalli, J., Quinn, D. M., Radi_, Z., Taylor, P., Velan, B., Kronman, C. and Shafferman, A. “Transition State Structure and Rate Determination for the Acylation Stage of Acetylcholinesterase Catalyzed Hydrolysis of (Acetylthio)choline” J. Am. Chem. Soc. 2000, 122, 2981-2987. Liang, Y., Medhekar, R., Brockman, H. L., Quinn, D. M. and Hui, D. Y. “Importance of Arginines 63 and 423 in Modulating the Bile Salt-Dependent and Bile Salt-Independent Hydrolytic Activities of Rat Carboxyl Ester Lipase” J. Biol. Chem. 2000, 275, 2404-24046. Malany, S., Baker, N. VerWeyst, M. Medhekar, R., Quinn, D. M., Velan, B., Kronman, C. and Shafferman, A. “Theoretical and Experimental Investigations of Electrostatic Effects on Acetylcholinesterase Catalysis and Inhibition” Chem. Biol. Interact 1999, 119-120, 99-110. Quinn, D.M.; Medhekar, R.; Baker, N. (1999) “Chapter 5: Ester Hydrolysis” in Comprehensive Natural Products Chemistry, Vol 5: Enzymes, Enzyme Mechanisms, Proteins, and Aspects of NO Chemistry (Poulter, C.D.; Ed.) Elsevier Science, Oxford, UK, pp 101-137. Malany, S.; Baker, N. VerWeyst, M. Medhekar, R.; Quinn, D. M.; Velan, B.; Kronman, C.; Shafferman, A. "Theoretical and Experimental Investigations of Electrostatic Effects on Acetylcholinesterase Catalysis and Inhibition" Chem.-Biol. Interact. 1999, 119-120, 99-110. Malany, S.; Sawai, M.; Sikorski, R. S.; Seravalli, J.; Quinn, D. M.; Radić, Z.; Taylor, P.; Velan, B.; Kronman, C.; Shafferman, A. “Transition State Structure and Rate Determination for the Acylation Stage of Acetylcholinesterase Catalyzed Hydrolysis of (Acetylthio)choline” J. Am. Chem. Soc. 1999, in press. Medhekar, R.; Baker, N.; Kearney, W.; Sando, K.; Quinn, D.M. “Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Esterases” (1998) in Structure and Function of Cholinesterases and Related Proteins (Doctor, B.P.; Quinn, D.M.; Rotundo, R.; Taylor, P., Eds.) Plenum Press, New York, p 233. Malany, S.; Sikorski, R. S.; Seravalli, J.; Medhekar, R.; Quinn, D.M.; Radić, Z.; Taylor, P.; Velan, B.; Kronman, C.; Shafferman, A. “Structure of the Acylation Transition State for Acetylcholinesterase Catalysis” (1998) in Structure and Function of Cholinesterases and Related Proteins (Doctor, B.P.; Quinn, D.M.; Rotundo, R. and Taylor, P.; Eds.) Plenum Press, New York, pp 197-202. Savle, P. S.; Medhekar, R. A.; Kelley, E. L.; May, J. G.; Watkins, S. F.; Fronczek, F. R.; Quinn, D. M.; Gandour, R. D. “Change in the Mode of Inhibition of Acetylcholinesterase by (4-Nitro)benzenesulfonoxy Derivatives of Conformationally Constrained Choline Analogs” Chem. Res. Toxicol. 1998, 11, 19-25. Quinn, D. M.; Feaster, S. R. “Esterases and Lipases” (1998) in Comprehensive Biological Catalysis (Sinnott, M., Ed.) Vol. 1; Academic Press, London, pp 455-482. Radić, Z.; Kirchhoff, P.; Quinn, D.M.; McCammon, J.A.; Taylor, P. “Electrostatic Influence on the Kinetics of Ligand Binding to Acetylcholinesterase: Distinctions Between Active Center Ligands and Fasciculin” J. Biol. Chem. 1997, 272, 23265-23277. Quinn, D.M. “Esterases of the α/β Hydrolase Fold Family” (1997) in Comprehensive Toxicology (Guengerich, F.P., Ed.) Vol. 3: Biotransformation; Elsevier Science, Oxford; pp 243-264. Saxena, A.; Maxwell, D.M.; Quinn, D.M.; Radić, Z.; Taylor, P.; Doctor, B.P. “Mutant Acetylcholinesterases as Potential Detoxification Agents for Organophosphate Poisoning” Biochem. Pharmacol. 1997, 54, 269-274. Feaster, S.R.; Quinn, D.M. “Mechanism-Based Inhibitors of Cholesterol Esterase” (1997) in Methods Enzymol. (Rubin, B. and Dennis, E.A.; Eds.) Academic Press, San Diego, pp 231-252. Feaster, S.R.; Quinn, D.M.; Barnett, B.L. “Molecular Modeling of the Structures of Human and Rat Pancreatic Cholesterol Esterases” Protein Sci. 1997, 6, 71-77. Feaster, S.R.; Lee, K.; Baker, N.; Hui, D.Y.; Quinn, D.M. “Molecular Recognition by Cholesterol Esterase of Active Site Ligands: Structure-Reactivity Effects for Inhibition by Aryl Carbamates and Subsequent Carbamylenzyme Turnover” Biochemistry 1996, 35, 16723-16734.10. Hosea, N.A.; Radić, Z.; Tsigelny, I.; Berman, H.A.; Quinn, D.M.; Taylor, P. “Aspartate 74 as a Primary Determinant in Acetylcholinesterase Governing Specificity to Cationic Organophosphonates” Biochemistry 1996, 35 10995-11004. Harel, M.; Quinn, D.M.; Nair, H.K.; Silman, I.; Sussman, J.L. “The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase” J. Am. Chem. Soc. 1996, 118, 2340-2346. Radić, Z.; Quinn, D.M.; Vellom, D.C.; Camp, S.; Taylor, P. “Allosteric Control of Acetylcholinesterase Catalysis by Fasciculin” J. Biol. Chem. 1995, 270, 20391-20399. Quinn, D.M.; Nair, H.K.; Seravalli, J.; Lee, K.; Arbuckle, T.; Radić, Z.; Vellom, D.; Pickering, N.; Taylor, P. “London Dispersion Interactions in Molecular Recognition by Acetylcholinesterase” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd., NewYork and London, pp 228-229. Quinn, D.M.; Seravalli, J.; Nair, H.K.; Medhekar, R.; Husseini, B.; Radić, Z.; Vellom, D.; Pickering, N.; Taylor, P. “The Function of Electrostatics in Acetylcholinesterase Catalysis” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd.; New York and London, pp 203-207. Sussman, J.L.; Harel, M.; Raves, M.; Quinn, D.M.; Nair, H.K.; Silman, I. “Structures of Complexes of Acetylcholinesterase with Covalently and Non-covalently Bound Inhibitors” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd., New York and London, pp 59-65. Ashani, Y.; Doctor, B.P.; Radić, Z.; Vellom, D.C.; Pickering, N.A.; Quinn, D.M.; Taylor, P. “Amino Acid Residues That Control Mono- and Bisquaternary Oxime-induced Reactivation of O-Ethyl Methylphosphonylated Cholinesterases” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd., New York and London, pp 133-140. Radić, Z.; Quinn, D.M.; Vellom, D.C.; Camp, S.; Taylor, P. “Amino Acid Residues in Acetylcholinesterase Which Influence Fasciculin Inhibition” (1995) in Enzymes of the Cholinesterase Family (Quinn, D.M.; Balasubramanian, A.S.; Doctor, B.P. and Taylor, P.; Eds.) Plenum Publishing Co. Ltd., New York and London, pp 183-188. Ashani, Y.; Radić, Z.; Tsigelny, I.; Vellom, D.C.; Pickering, N.A.; Quinn, D.M.; Doctor, B.P.; Taylor, P. “Amino Acid Residues Controlling Reactivation of Organophosphonyl Conjugates of Acetylcholinesterase by Mono- and Bisquaternary Oximes” J. Biol. Chem. 1995, 270, 6370-6380. Sussman, J.L.; Harel, M.; Raves, M.; Quinn, D.; Silman, I. “3-D Structure of Acetylcholinesterase and Its Complexes with Anticholinesterase Agents” (1995) in Modeling of Biomolecular Structures and Mechanisms (A. Pullman et al.; Eds.) Kluwer Academic Publishers, The Netherlands, 455-460.