PUBLICATIONS (complete)

Research Papers

(1)  Cook, P. F. and Wedding, R. T.:  A Reaction Mechanism from Steady-State Kinetic Studies for O-Acetylserine Sulfhydrylase from Salmonella typhimurium LT-2.  J. Biol. Chem. 251, 2023-2029 (1976).

(2)  Cook, P,. F. and Wedding, R. T.:  Initial Kinetic Characterization of the Multienzyme Complex, Cysteine Synthetase.  Arch. Biochem. Biophys. 178, 293-302 (1977).

(3)  Cook, P. F. and Wedding, R. T.:  Overall Mechanism and Rate Equation for O-Acetylserine Sulfhydrylase, J. Biol. Chem. 252, 3549 (1977).

(4)  Cook, P. F. and Wedding, R. T.:  Cysteine Synthetase from Salmonella typhimurium LT-2:  Aggregation, Kinetic Behavior and Effect of Modifiers.  J. Biol. Chem. 253, 7874-7879 (1978).

(5)  Viola, R. E., Cook, P. F. and Cleland, W. W.:  Preparation and Purification of Stereospecifically Deuterated (4-2H)-Nicotinamide Adenine Nucleotides.  Anal. Biochem. 96, 334-340 (1979).

(6)  Cook, P. F., Blanchard, J. S. and Cleland, W. W.:  Primary and Secondary Deuterium Isotope Effects on the Equilibrium Constant for Enzyme Catalyzed Reactions.  Biochemistry 19, 4853-4858 (1980).

(7)  Cook, P. F., Kenyon, G. L. and Cleland, W. W.:  Use of pH Studies to Elucidate the Catalytic Mechanism of Rabbit Muscle Creatine Kinase.  Biochemistry 20, 1204-1210 (1981).

(8)  Cook, P. F. and Cleland, W. W.:  Mechanistic Deductions from Isotope Effects in Multireactant Enzyme Mechanisms.  Biochemistry 20, 1790-1796 (1981).

(9)  Cook, P. F. and Cleland, W. W.:  pH Variation of Isotope Effects.  I. Isotope and pH Dependent Step the Same.  Biochemistry 20, 1797-1805 (1981).

(10)  Cook, P. F. and Cleland, W. W.:  pH Variation of Isotope Effects.  II. Isotope Dependent Step Not pH Dependent.  Kinetic Mechanism and Alcohol Dehydrogenase.  Biochemistry 20, 1805-1816 (1981).

(11)  Cook, P. F., Oppenheimer, N. J. and Cleland, W. W.:  Secondary Deuterium and Nitrogen-15 Isotope Effects in Enzyme-Catalyzed Reactions.  Chemical Mechanism of Liver Alcohol Dehydrogenase.  Biochemistry 20, 1817-1825 (1981).

(12)  Grimshaw, C. E., Cook, P. F. and Cleland, W. W.:  The Chemical Mechanism of Bacillus subtilis Alanine Dehydrogenase.  Biochemistry 20, 5650-5655 (1981)

(13)  Cook, P. F.:  Kinetic Studies to Determine the Mechanism of Regulation of Bovine Liver Glutamate Dehydrogenase by Nucleotide Effectors.  Biochemistry 21, 113-116 (1982).

(14)  Cook, P. F., Neville, M. E., Vrana, K. F., Hartl, F. T. and Roskoski, R. Jr.:  Cyclic 3',5'-Adenosine Monophosphate Dependent Protein Kinase:  Kinetic Mechanism for the Bovine Skeletal Muscle Catalytic Subunit.  Biochemistry 21, 5794-5799 (1982).

(15)  Kiick, D. M. and Cook, P. F.:  pH Studies Toward the Elucidation of the Auxiliary Catalyst of Pig Heart Aspartate Aminotransferase.  Biochemistry 22, 375-382 (1983).

(16)  Taylor, K. B., Cook, P. F. and Cleland, W. W.:  Solvent Isotope Effects on the Reaction Catalyzed by Yeast Hexokinase.  Eur. J. Biochem. 134, 571-574 (1983).

(17)  Reinhardt, R. R., Wecker, L. and Cook, P. F.:  Kinetic Mechanism of Choline Kinase from Rat Striata.  J. Biol. Chem. 259, 7446-7452 (1984).

(18)  Bertagnolli, B. L. and Cook, P. F.:  Kinetic Mechanism of Pyrophosphate-Dependent Phosphofructokinase from Propionibacterium freudenreichii.  Biochemistry 23, 4101-4108 (1984).

(19)  Nuiry, I. I., Hermes, J. D., Weiss, P. M., Chen, C. Y. and Cook, P. F.:  Kinetic Mechanism and Location of Rate Determining Steps for Aspartase from Hafnia alvei.  Biochemistry 23, 5168-5175 (1984).

(20)  Park, S. H., Kiick, D. M., Harris, B. G. and Cook, P. F.:  NAD-Malic Enzyme from Ascaris suum:  Kinetic Mechanism in the Direction of Oxidative Decarboxylation.  Biochemistry 23, 5446-5453  (1984).

(21)  Kiick, D. M., Allen, B. L., Rao, J.G.S., Harris, B. G. and Cook, P. F.:  Determination of Dissociation Constants for Enzyme-Reactant Complexes for NAD-Malic Enzyme from Ascaris suum Using Modulation of the Thiol Inactivation Rate.  Biochemistry 23, 5454-5459 (1984).

(22)  Roskoski, R. Jr., Reinhardt, R. R., Enseleit, W., Johnson, W. D. and Cook, P. F.:  Cardiac Cholinergic Muscarinic Receptors:  Changes in Multiple Affinity Forms with Down Regulation.  J. Pharm. Exp. Ther. 232, 754-759 (1985).

(23)  Nuiry, I. I. and Cook, P. F.:  The pH Dependence of the Reductive Carboxylation of Pyruvate by Malic Enzyme.  Biochim. Biophys. Acta 829, 295-298 (1985).

(24)  Rao, G.S.J., Harris, B. G. and Cook, P. F.:  Diethylpyrocarbonate Inactivation of NAD-Malic Enzyme from Ascaris suum.  Arch. Biochem. Biophys. 241, 67-74 (1985).

(25)  Kiick, D. M., Harris, B. G. and Cook, P. F.:  Protonation Mechanism and Location of Rate Determining Steps for the Ascaris suum NAD-Malic Enzyme Reaction from Isotope Effects and pH Studies.  Biochemistry 25, 227-236 (1986).

(26)  Park, S.-H., Harris, B. G. and Cook, P. F.:  pH Dependence of the Kinetic Parameters for the Oxalacetate Decarboxylation and Pyruvate Reduction Reactions Catalyzed by Malic Enzyme.  Biochemistry 25, 3752-3759 (1986).

(27)  Bertagnolli, B. L., Younathan, E. S., Voll, R. J., Pittman, C. E. and Cook, P. F.:  Carbohydrate and Substrate Specificity of Bacterial and Plant Pyrophosphate-Dependent Phosphofructokinases.  Biochemistry 25, 4674-4681 (1986).

(28)  Bertagnolli, B. L., Younathan, E. S., Voll, R. J. and Cook, P. F.:  Kinetic Studies on the Activation of Pyrophosphate-Dependent Phosphofructokinase from Mung Bean by Fructose 2,6-bisphosphate and Related Compounds.  Biochemistry 25, 4682-4687 (1986).

(29)  Rao, G.S.J., Harris, B. G. and Cook, P. F.:  Modification of an Arginine Residue Essential for the Activity of NAD-Malic Enzyme from Ascaris suum.  Arch. Biochem. Biophys. 255, 8-13 (1987).

(30)  Yoon, M.-Y. and Cook, P. F.:  Chemical Mechanism of the Cyclic 3',5'-Monophosphate-Dependent Protein Kinase from pH Studies.  Biochemistry 26, 4118-4125 (1987).

(31)  Cook, P. F., Rao, G.S.J., Hofer, H. W. and Harris, B. G.:  Correlation Between Hysteresis and Allosteric Properties for Phosphofructokinase from Ascaris suum.  J. Biol. Chem. 262, 14063-14067 (1987).

(32)  Rao, G.S.J., Wariso, B. A., Cook, P. F., Hofer, H. W. and Harris, B. G.:  Reaction of Ascaris suum Phosphofructokinase with Diethylpyrocarbonate:  Inactivation and Desensitization to Allosteric Modulation.  J. Biol. Chem. 262, 14068-14073 (1987).

(33)  Rao, G.S.J., Harris, B. G. and Cook, P. F.:  Kinetic Mechanism of Ascaris suum Phosphofructokinase Desensitized to Allosteric Modulation by Diethylpyrocarbonate Modification.  J. Biol. Chem. 262, 14074-14079 (1987).

(34)  Weiss, P. M., Cook, P. F., Hermes, J. D. and Cleland, W. W.:  Evidence from 15N and Solvent Deuterium Isotope Effects on the Chemical Mechanism of Adenosine Deaminase.  Biochemistry 26, 7378-7384 (1987).

(35)  Chen, C.-Y., Harris, B. G. and Cook, P. F.:  Isotope Partitioning for NAD-Malic Enzyme from Ascaris suum Confirms a Steady-State Random Mechanism.  Biochemistry 27, 212-219 (1988).

(36)  Weiss, P. M., Garcia, G. A., Kenyon, G. L., Cleland, W. W. and Cook, P. F.:  Kinetics and Mechanism of Benzoylformate Decarboxylase Using ¹³C and Solvent Deuterium Isotope Effects on Benzoylformate and Benzoylformate Analogues.  Biochemistry 27, 2197-2265 (1988).

(37)  Bhatnagar, A., Das, B., Gavva, S. R., Cook, P. F. and Srivastava, S. K.:  The Kinetic Mechanism of Human Placental Aldose Reductase and Aldehyde Reductase II.  Arch. Biochem. Biophys. 261, 264-274 (1988).

(38)  Cho, Y.-K. and Cook, P. F.:  Inactivation of Pyrophosphate-Dependent Phosphofructokinase from Propionibacterium freudenreichii by Pyridoxal 5'-Phosphate:  Determination of the pH Dependence of Enzyme-Reactant Dissociation Constants from Protection Against Inactivation.  J. Biol. Chem.  263, 5135-5140 (1988)

(39)  Cho, Y.-K., Matsunaga, T., Kenyon, G. L., Bertagnolli, B. L. and Cook, P. F.:  Isotope Exchange as a Probe of the Kinetic Mechanism of Pyrophosphate-Dependent Phosphofructokinase.  Biochemistry 27, 3320-3325 (1988).

(40)  Kong, C.-T. and Cook, P. F.:  Isotope Partitioning in the Adenosine 3',5'-Monophosphate Dependent Protein Kinase Reaction Indicates a Steady-State Random Kinetic Mechanism.  Biochemistry  27, 4795-4799 (1988).

(41)  Cini, J. K., Cook, P. F. and Gracy, R. W.:  Molecular Basis for the Isozymes of Bovine Glucose 6-Phosphate Isomerase.  Arch. Biochem. Biophys. 263, 93-106 (1988).

(42)  Weiss, P. M., Chen, C.-Y., Cleland, W. W. and Cook, P. F.:  Primary Deuterium and ¹⁵N Isotope Effects as a Mechanistic Probe of Alanine and Glutamate Dehydrogenases. Biochemistry 27, 4814-4822 (1988).

(43)  Cho, Y.-K., and Cook, P. F.:  pH Dependence of Kinetic Parameters for the Pyrophosphate-Dependent Phosphofructokinase from Propionibacterium freudenreichii.  Biochemistry  28, 4155-4160 (1989).

(44)  Park, S.-H., Harris, B. G. and Cook, P. F.:  Substrate Activation Induced by Oxalate in the NAD-Malic Enzyme Reaction.  Biochemistry  28, 6334-6338 (1989).

(45)  Park, S.-H., and Cook, P. F.:  Appendix:  Derivation of the Rate Equation Describing Substrate Activation by L-Malate Induced by Oxalate in the NAD-Malic Enzyme Reaction.  Biochemistry 28, 6338-6340 (1989).

(46)  Podschun, B., Wahler, G., Cook, P. F. and Schnackerz, K. D.:  Kinetic Mechanism of Dihydropyrimidine Dehydrogenase from Pig Liver. J. Biol. Chem. 265, 12966-12972 (1990).

(47)  Hara, S., Payne, M. A., Schnackerz, K. D., and Cook, P. F.:  A Rapid Purification Procedure and a Computer Assisted Sulfide Ion Selective Electrode Assay for O-Acetylserine Sulfhydrylase from Salmonella typhimurium.  Protein Expression and Purification. 1, 70-76 (1990).

(48)  Mallick, S., Harris, B. G., and Cook, P. F.:  Kinetic Mechanism of the Ascaris suum NAD-Malic Enzyme in the Direction of Reductive Carboxylation of Pyruvate. J. Biol. Chem. 266, 2732-2738 (1991).

(49)  Rao, G. S. J., Cook, P. F., and Harris, B. G.:  Evidence for Conformational Transitions in the Phosphofructokinase from Ascaris suum:  Fluorescence and Circular Dichroism Studies.  J. Biol. Chem. 266, 8884-8890 (1991).

(50)  Payne, M. A., Harris. B.G., and Cook, P.F.:  Fructose 2,6-Bisphosphate and AMP Increase the Affinity of the Ascaris suum Phosphofructokinase for Fructose 6-Phosphate in a Process Separate from the Relief of ATP Inhibition.  J. Biol. Chem. 266, 8891-8896 (1991).

(51)  Payne, M. A., and Cook, P. F.:  Appendix.  Derivation of the Rate Equation for Competitive Activation by Effectors.  J. Biol. Chem. 266, 8897-8898 (1991).

(52)  Weiss, P. M., Gavva, S. R., Urbauer, J., Harris, B. G., Cleland, W. W., and Cook, P. F.:  Multiple Isotope Effects With Alternative Dinucleotide Substrates as a Probe of the Malic Enzyme Reaction.  Biochemistry 30, 5755-5763 (1991).

(53)  Gavva, S. R., Weiss, P. M., Harris, B. G., and Cook, P. F.:  Modification of a Thiol at the Active Site of the Ascaris suum NAD-Malic Enzyme Results in Changes in the Rate Determining Steps for Oxidative Decarboxylation of Malate.  Biochemistry 30, 5764-5769 (1991).

(54)  Rao, G. S. J., Cook, P. F., and Harris, B. G.:  Modification of the ATP Inhibitory Site of the Ascaris suum Phosphofructokinase Results in the Stabilization of an Inactive T-State.  Biochemistry 30, 9998-10004 (1991).

(55)  Cook, P. F., Nalabolu, S. R., and Tai, C.-H.:  Mechanism of O-Acetylserine Sulfhydrylase from Salmonella typhimurium.  Amino Acids 2, 119-125 (1992).

(56)  Cook, P. F., Hara, S., Nalabolu, S., and Schnackerz, K. D.:  pH Dependence of the Absorbance and ³¹P NMR Spectra of O-Acetylserine Sulfhydrylase in the Absence and Presence of O-Acetyl-L-Serine.  Biochemistry 31, 2298-2303 (1992).

(57)  Clancy, L. L., Rao, G. S. J., Finzel, B. C., Muchmore, S. W., Holland, D. R., Watenpaugh, K. D., Krishnamurthy, H. M., Sweet, R. M., Cook, P. F., Harris, B. G., and Einspahr, H. M.:  Crystallization of the NAD-dependent Malic Enzyme from the Parasitic Nematode Ascaris suum. J. Mol. Biol. 226, 565-569 (1992).

(58)  Qamar, R., Yoon, M.-Y., and Cook, P. F.:  Kinetic Mechanism of the Adenosine 3'.5'-Monophosphate Dependent Protein Kinase Catalytic Subunit in the Direction of MgADP Phosphorylation.  Biochemistry 31, 9986-9992 (1992).

(59)  Lai, C.-J., Harris, B. G., and Cook, P. F.:  Mechanism of Activation of the NAD-Malic Enzyme from Ascaris suum by Fumarate. Arch. Biochem. Biophys. 299, 214-219 (1992).

(60)  Kulkarni, G., Cook, P. F., and Harris, B. G.:  Cloning and Sequencing of the NAD-Malic Enzyme from Ascaris suum. Arch. Biochem. Biophys. 300, 231-237 (1993).

(61)  Cook, P. F., Yoon, M.-Y., Hara, S., and McClure, G. D.:  Dependence of Isotope Effects on the Concentration of Products. Biochemistry 32, 1795-1807 (1993).

(62)  Rajapaksa, R., Abu-Soud, H., Raushel, F. M., Harris, B. H., and Cook, P.F.:  Pre-Steady State Kinetics Reveal a Slow Isomerization of the Enzyme-NAD Complex in the NAD-Malic Enzyme Reaction. Biochemistry 32, 1928-1934 (1993).

(63)  Berdis, A. J., and Cook, P. F.:  Overall Kinetic Mechanism of 6-Phosphogluconate Dehydrogenase from Torula.  Biochemistry 32, 2036-2040 (1993).

(64)  Berdis, A. J., and Cook, P. F.:  Chemical Mechanism of 6-Phosphogluconate Dehydrogenase from Torula.  Biochemistry 32, 2041-2046 (1993).

(65)  Podschun, B., Jahnke, K., Schnackerz, K. D., and Cook, P. F.:  Acid-Base Catalytic Mechanism of the Dihydropyrimidine Dehydrogenase from Pig Liver. J. Biol. Chem. 268, 3407-3413 (1993).

(66)  Jahnke, K., Podschun, B., Schnackerz, K. D., Kautz, J., and Cook, P. F.:  Acid-Base Chemical Mechanism of Dihydropyrimidinase from pH Studies. Biochemistry 32, 5160-5166 (1993).

(67)  Tai, C.-H., Nalabolu, S. R., Jacobson, T. M., Minter, D. E., and Cook, P. F.:  Kinetic Mechanisms of O-Acetylserine Sulfhydrylases A and B from Salmonella typhimurium with Natural and Alternate Substrates. Biochemistry 32, 6433-6442 (1993).

(68)  McClure, G. D., Qamar, R., and Cook, P. F.:  A Method for Counting Active Sites of Cyclic AMP-Dependent Protein Kinase. J. Enz. Inhib. 7, 151-157 (1993).

(69)  Rao, J. G. S., Goldsmith, E. J., Mottonen, J., and Cook, P. F.:  Crystallization and Preliminary X-ray Data for the A-Isozyme of O-Acetylserine Sulfhydrylase from Salmonella typhimurium. J. Mol. Biol. 231, 1130-1132 (1993).

(70)  Qamar, R., and Cook, P. F.:  Acid-Base Chemical Mechanism of the Cyclic AMP-Dependent Protein Kinase Catalytic Subunit in the Direction of MgADP Phosphorylation. Biochemistry 32, 6802-6806 (1993).

(71)  Berdis, A. J., and Cook, P. F.:  The 2’-Phosphate of NADP is Critical for Optimum Binding and Catalysis in the 6-Phosphogluconate Dehydrogenase Reaction. Arch. Biochem. Biophys. 305, 551-558 (1993).

(72)  Yang, C.-H., Qamar, R., Minter, D., Norton, S. J., and Cook, P. F.:  Synthesis and Isolation of a Diastereomeric pair of Phosphonopeptide Inhibitors of Cyclic AMP-Dependent Protein Kinase. Tetrahedron 50, 1919-1926 (1994).

(73)  Bertagnolli, B. L., and Cook, P. F.:  Lanthanide Pyrophosphates as Substrates for the Pyrophosphate-Dependent Phosphofructokinases from Propionibacterium freudenreichii and Phaseolus aureus.  Evidence for Two Divalent Metal Ions Required for Reaction. Biochemistry 33, 1663-1667 (1994).

(74)  McClure, G. D., and Cook, P. F.:  Product Binding to the a-Carboxyl Subsite Results in a Conformational Change at the Active Site of O-Acetylserine Sulfhydrylase-A:  Evidence from Fluorescence Spectroscopy. Biochemistry 33, 1674-1683 (1994).

(75)  Karsten, W. E., and Cook, P. F.:  Stepwise versus Concerted Oxidative Decarboxylation Catalyzed by Malic Enzyme:  A Reinvestigation. Biochemistry 33, 2096-2103 (1994).

(76)  Leu, L.-S., and Cook, P. F.:  Kinetic Mechanism of Serine Transacetylase from Salmonella typhimurium. Biochemistry 33, 2667-2671 (1994).

(77)  DeLucas, L. J., Long, M. M., Moore, K. M., Rosenblum, T. L., Bray, T. L., Smith, C., Carson, M., Narayana, S. V. L., Harrington, M. D., Carter, D., Clark, A. D., Jr., Nanni, R. G., Ding, J., Jacobo-Molina, A., Kamer, G., Hughes, S. H., Arnold, E., Einspahr, H. M., Clancy, L. L., Rao, G., S. J., Cook, P. F., Harris, B. G., Munson, S. H., Finzel, B. C., McPherson, A., Weber, P. C., Lewandowski, F. A., Nagabhushan, T. L., Trotta, P. P., Reichert, P., Naiva, M. A., Wilson, K. P., Thomson, J. A., Richards, R. N., Bowersox, K. D., Meade, C. J., Baker, E. S., Bishop, S. P., Dunbar, B. J., Trinh, E., Prahl, J., Sacco, A., Jr., and Bugg, C. E.:  Recent Results and New Hardware Developments for Protein Crystal Growth in Microgravity. J. Crys. Growth 135, 183-195 (1994).

(78)  Leu, L.-S., and Cook, P. F.:  Formation of an Acetylenzyme Intermediate in the Reaction Catalyzed by Serine Transacetylase. Pr. and Pep. Lett. 1, 157-163 (1994).

(79)  Karsten, W. E., Gavva, S. R., Park, S.-H., and Cook, P. F.:  Metal Ion Activator Effects on Intrinsic Isotope effects for Hydride Transfer and Decarboxylation Catalyzed by the NAD-Malic Enzyme from Ascaris suum. Biochemistry 34, 3253-3260 (1995).

(80)  Yoon, M.-Y., Thayer-Cook, K. A., Berdis, A. J., Karsten, W. E., Schnackerz, K. D., and Cook, P. F.:  Acid-Base Chemical Mechanism of the Aspartase from Hafnia alvei. Arch. Biochem. Biophys. 320, 115-122 (1995).

(81)  Payne, M. A., Harris, B. G., and Cook, P. F.:  Acid-Base Catalytic Mechanism and pH Dependence of Fructose 2,6-Bisphosphate Activation of the Acsaris suum Phosphofructokinase. Biochemistry 34, 7782-7787 (1995).

(82)  Karsten, W. E., Lai, C.-J, Gavva, S. R., and Cook, P. F.:  Inverse Solvent Deuterium Isotope Effects in the NAD-Malic Enzyme Reaction are the Result of the Viscosity Difference Between H₂O and D₂O:  Implications for Solvent Deuterium Isotope Effect Studies. J. Am Chem. Soc. 117, 5914-5918 (1995).

(83)  Einspahr, H. M., DeLucas, L. J., Clancy, L. L., Finzel, B. C., Rao, J., Cook, P. F., Harris, B. G., and Munson, S. H.:  Glovebox Experiments with Malic Enzyme on USML-1. AIP Conf. Proc. 325, 193-197 (1995).

(84)  Schnackerz, K. D., Tai, C.-H., Simmons, J. W., III, Jacobson, T. M., Rao, G. S. J., and Cook, P. F.:  Identification and Characterization of the External Aldimine Intermediate of the O-Acetylserine Sulfhydrylase Reaction. Biochemistry 34, 12152-12160 (1995).

(85)  Rao, G. S. J., Schnackerz, K. D., Harris, B. G., and Cook, P. F.:  Circular Dichroism as a Probe of a pH-Dependent Allosteric Transition in the Phosphofructokinase from Ascaris suum. Arch. Biochem. Biophys. 322, 410-416 (1995).

(86)  Tai, C.-H., Nalabolu, S. R., Jacobson, T. M., Simmons, J. W., III, and Cook, P. F.:  pH Dependence of Kinetic Parameters for O-Acetylserine Sulfhydrylases A and B from Salmonella typhimurium. Biochemistry 34, 12311-12322 (1995).

(87)  Schnackerz, K. D., and Cook, P. F.:  Resolution of the Pyridoxal 5’-Phosphate from O-Acetylserine Sulfhydrylase and Reconstitution with the Native Cofactor and Analogs. Arch. Biochem. Biophys. 324, 71-77 (1995).

(88)  Lagueux, J., Menard, L., Candas, B., Brochu, G., Potvin, F., Verreault, A., Cook, P. F., Poirier, G. G.:  Equilibrium Model in an in vitro poly(ADP-ribose) Turnover System. Biochim. Biophys. Acta 1264, 201-208 (1995).

(89)  Treptau, T., Piram, P., Cook, P. F., Rodriguez, R., Hoffmann, R., Jung, S., Thalhoher, H. P., Harris, B. G., and Hofer, H. W.:  Comparison of the Substrate Specificities of cAMP-Dependent Protein Kinase from Bovine Heart and Ascaris Muscle. Biological Chemistry Hoppe Seyler 377, 203-209 (1996).

(90)  Woehl, E., Tai, C.-H., Dunn, M. F., and Cook, P. F.:  Rapid Scanning Stopped-Flow Studies of O-Acetylserine Sulfhydrylase Indicate a Rate-Determining First Half Reaction. Biochemistry 35, 4776-4783 (1996).

(91)  Gibson, G., Harris, B. G., and Cook, P. F.:  Intermediate Partitioning Indicates MgATP Binding to the Ascaris suum Phosphofructokinase Prior to Fructose 6-Phosphate is Highly Preferred. Biochemistry 35, 5451-5457 (1996).

(92)  Hwang, C.-C., Woehl, E. U., Dunn, M. F., and Cook, P. F.:  Kinetic Isotope Effects as a Probe of the b-Elimination Reaction Catalyzed by O-Acetylserine Sulfhydrylase. Biochemistry 35, 6358-6365 (1996).

(93)  Strambini, G., Cioni, P., and Cook, P. F.:  Tryptophan and Coenzyme Luminescence as a Probe of Conformation Along the O-Acetylserine Sulfhydrylase Reaction Pathway. Biochemistry 35, 8392-8400 (1996).

(94)  Schmitt, U., Cook, P. F., and Schnackerz, K. D..:  Characterization and Mechanism of Dihydropyrimidine Dehydrogenase from Alcaligenes eutrophus. Arch. Biochem. Biophys. 332, 175-182 (1996).

(95)  Tipton, P. A., Quinn, T. P., Peisach, J., and Cook, P. F.:  Determnination of the Conformation of L-Malate in Binary Complex with the Ascaris suum malic enzyme:  An ESEEM Study. Protein Science 5, 1648-1654 (1996).

(96)  Rege, V., Tai, C.-H., Kredich, N. M., Karsten, W. E., Schnackerz, K. D., and Cook, P. F.:  A Change in the Internal Aldimine Lysine (K42) in O-Acetylserine Sulfhydrylase to Alanine Indicates a Role for the Lysine in Transimination and as a General Base Catalyst. Biochemistry 35, 13485-13493 (1996).

(97)  Khayer, K., Akhtar, M., Wilkie, J., Gani, D., Jung, H., Schnackerz, K. D., and Cook, P. F.:  The Aspartate a-Amine pK Decreases Upon Binding to Aspartate Aminotransferase as a Result of Partial Charge Neutralization at the a- and b-Carboxylates. Pr, & Pep. Ltrs. 3, 309-314 (1996).

(98)  Cook, P. F., Tai, C.-H., Hwang, C.-C. Woehl, E. U., Dunn, M. F., and Schnackerz, K. D.:  Substitution of Pyridoxal 5’-Phosphate in the O-Acetylserine Sulfhydrylase from Salmonella typhimurium by Cofactor Analogs Provides an Effective Test of the Mechanism of a-Aminoacrylate Formation. J. Biol. Chem. 271, 25842-25849 (1996).

(99)  Price, N. E., and Cook, P. F.:  Kinetic and Chemical Mechanisms of the 6-Phosphogluconate Dehydrogenase from Sheep Liver. Arch. Biochem. Biophys. 336, 215-223 (1996).

(100) Chooback, L., Karsten, W. E., Nalabolu, S. R., Kulkarni, G., Harris, B. G., and Cook, P. F.:  Expression, Purification, and Characterization of Recombinant NAD-Malic Enzyme from Ascaris suum. Protein Expression and Purification. 10, 51-54 (1997).

(101) Rosenbaum, K., Schaffrath, B., Hagen, W. R., Jahnke, K., Cook, P. F., and Schnackerz, K. D.:  Purification, Characterization, and Kinetics of Recombinant Dihydropyrimidine Dehydrogenase from Escherichia coli Protein Expression and Purification. 10, 185-191 (1997).

(102) Mizuguchi, H., Cook, P. F., Hasemann, C. A., and Uyeda, K.: Chemical Mechanism of the Fru 6-P,2-Kinase Reaction from the pH Dependence of Kinetic Parameters of Site-Directed Mutants of Active Site Basic Residues. Biochemistry 36, 8775-8784 (1997).

(103) Benci, S., Vaccari, S., Mozzarelli, A., and Cook, P. F.: Time-Resolved Fluorescence of O-Acetylserine Sulfhydrylase Catalytic Intermediates Biochemistry 36, 15419-15427 (1997).

(104) Cook, P. F.: Mechanism from Isotope Effects. Isotopes in Environmental and Health Sciences 34, 3-17 (1998).

(105) Chooback, L., Price, N. E., Karsten, W. E., Nelson, J., Sundstrom, P. R., and Cook, P. F.: Cloning, Expression, Purification, and Characterization of the 6-Phosphogluconate Dehydrogenase from Sheep Liver. Protein Expression and Purification. 13, 251-258 (1998).

(106) Rosenbaum, K., Jahnke, K., Schnackerz, K. D., and Cook, P. F.: Secondary Tritium and Solvent Deuterium Kinetic Isotope Effects as a Probe of the Dihydropyrimidine Dehydrogenase Reaction. Biochemistry 37, 9156-9159 (1998).

(107) Burkhard, P., Rao, G. S. J., Hohenester, E., Schnackerz, K. D., Cook, P. F., and Jansonius, J. N.: The Three-dimensional Structure of O-Acetylserine Sulfhydrylase from Salmonella typhimurium at 2.2 Å. J. Mol. Biol. 283, 111-120 (1998).

(108) Mozzarelli, A., Bettati, S., Pucci, A. M., and Cook, P. F.: The Catalytic Competence of O-Acetylserine Sulfhydrylase in the Crystal Probed by Polarized Absorption Microspectrophotometry. J. Mol. Biol. 283, 121-133 (1998).

(109) Tai, C.-H., Yoon, M.-Y., Rege, V. D., Kredich, N. M., Schnackerz, K. D., and Cook, P. F.: Cysteine-42 Is Important for Maintaining an Integral Active Site for O-Acetylserine Sulfhydrylase Resulting in the Stabilization of the a-Aminoacrylate Intermediate. Biochemistry 37, 10597-10604 (1998).

(110) Hwang, C.-C., Berdis, A. J., Karsten, W. E., Cleland, W. W., and Cook, P. F.: Oxidation of 6-Phosphogluconate by 6-Phosphogluconate Dehydrogenase Proceeds by a Stepwise Mechanism with NADP and APADP as Oxidants. Biochemistry 37, 12596-12602 (1998)

(111) Karsten, W. E., Chooback, L., and Cook, P. F.: Glutamate 190 is a General Acid in the 6-Phosphogluconate Dehydrogenase-Catalyzed Reaction. Biochemistry 37, 15698-15702 (1998).

(112) Hwang, C.-C., and Cook, P. F.: Multiple Isotope Effects as a Probe of Proton and Hydride Transfer in the 6-Phosphogluconate Dehydrogenase Reaction. Biochemistry 37, 15691-15697 (1998).

(113) Benci, S., Vaccari, S., Mozzarelli, A., and Cook, P. F.: Time-Resolved Fluorescence of O-Acetylserine Sulfhydrylase. Biochim. Biophys. Acta 1429, 317-330 (1999).

(114) Mizuguchi, H., Cook, P. F., Tai, C.-H., Hasemann, C. A., and Uyeda, K.: Reaction Mechanism of the Fructose 2,6-Bisphosphatase: Mutation of the Covalent Catalyst, Histidine 256, Forces a Back-up Alternative Pathway. J. Biol. Chem. 274, 2161-2175 (1999).

(115) Yuen, M. H., Mizuguchi, H., Lee, Y.-H., Cook, P. F., Uyeda, K., and Hasemann, C. A.: Crystal Structure of the H256A Mutant of Rat Testis Fructose 6-phosphate, 2-kinase/Fructose 2,6-Bisphosphatase: Fructose 6-phosphate in the Active Site Leads to Mechanisms for Both Mutant and Wild Type Bisphosphatase Activities. J. Biol. Chem. 274, 2176-2185 (1999).

(116) Benci, S., Bettati, S., Vaccari, S., Schianchi, G., Cook, P. F., and Mozzarelli, A.: O-Acetylserine Sulfhydrylase Probed by Static and Time-Resolved Tryptophan Fluorescence During Catalysis. J. Photochem. Photobiol. 48, 17-26 (1999).

(117) Karsten, W. E., Hwang, C.-C., and Cook, P. F.: a-Secondary Deuterium Kinetic Isotope Effects Indicate Hydrogen Tunneling and Coupled Motion in the Oxidation of L-Malate by NAD-Malic Enzyme. Biochemistry 38, 4398-4402 (1999).

(118) Rao, G. S. J., Harris, B. G., and Cook, P. F.: Kinetic Characterization of a Stabilized T-State of the Phosphofructokinase from Ascaris suum. Arch. Biochem. Biophys. 365, 335-343 (1999).

(119) Burkhard, P., Tai, C.-H., Ristroph, C., Cook, P. F., and Jansonius, J. N.: Ligand Binding Induces a Large Conformational Change: A Molecular Switch in O-Acetylserine Sulfhydrylase. J. Mol. Biol. 291, 941-953 (1999).

(120) Zhang, L., Chooback, L., and Cook, P. F.: Lysine 183 is a General Base in the 6-Phosphogluconate Dehydrogenase-Catalyzed Reaction. Biochemistry 38, 11231-11238 (1999).

(121) Karsten, W. E., Chooback, L., Liu, D., Hwang, C.-C., Lynch, C. R., and Cook, P. F.: Mapping the Active Site Topography of the NAD-Malic Enzyme vis Site-Directed Mutagenesis. Biochemistry 38, 10527-10532 (1999).

(122) Ehrlich, J., Hwang, C.-C., Cook, P. F., and Blanchard, J. S.: Evidence for a stepwise Mechanism of the OMP Decarboxylase. J. Am. Chem. Soc. 121, 6966-6967 (1999).

(123) Schnackerz, K. D., Tai, C.-H., Pötsch, R. K. W., and Cook, P. F.: Substitution of Pyridoxal 5’-Phosphate in D-Serine Dehydratase from Escherichia coli by Cofactor Analogues Provides Information on Cofactor Binding and Catalysis. J. Biol. Chem. 274, 36935-36943. (1999).

(124) Stanley, T., Johnson, W. H., Jr., Burks, E. A., Whitman, C., Hwang, C.-C., Cook, P. F. (1999): Kinetic, Stereochemical, and Isotope Effect Studies of 4-Oxalocrotonate Decarboxylase in the 4-Oxalocrotonate Decarboxylase/Vinylpyruvate Hydratase Complex. Biochemistry 39, 718-726 (2000).

(125) Tai, C.-H., Cook, P. F., and Schnackerz, K. D.: Conformation of the a-Aminoacrylate Intermediate of O-Acetylserine Sulfhydrylase from Salmonella typhimurium as Inferred from ³¹P NMR Spectroscopy. Pr. & Pep. Ltrs. 7, 207-210 (2000).

(126) Liu, D., Karsten, W. E., and Cook, P. F.: Lysine 199 is the General Acid in the NAD-Malic Enzyme Reaction. Biochemistry 39, 11955-11960 (2000).

(127) Burkhard, P., Tai, C.-H., Jansonius, J. N., and Cook, P. F.: Conformational Changes Regulate the Activity of O-Acetylserine Sulfhydrylase. J. Mol. Biol. 303, 279-286 (2000).

(128) Karsten, W. E., and Cook, P. F.: Pyridine Nucleotide-Dependent b-Hydroxyacid Oxidative Decarboxylases: An Overview. Pr. & Pep. Ltrs. 7, 281-286 (2000).

(129) Rao, G. S. J., Coleman, D. E., Kulkarni, G., Goldsmith, E. J., Cook, P. F., and Harris, B. G.: NAD-Malic Enzyme from Ascaris suum: Sequence and Structural Studies. Pr. & Pep. Ltrs. 7, 297-304 (2000).

(130) Zhang, L. and Cook, P. F.: Mechanism of 6-Phosphogluconate Dehydrogenase. Pr. & Pep. Ltrs. 7, 313-322 (2000).

(131) Tai, C.-H., and Cook, P. F.: Mechanism of the b-Replacement Reaction Catalyzed by O-Acetylserine Sulfhydrylase. Accts. Chem. Res. 34, 49-59 (2001).

(132) Sakurai, M., Haseman, C. A., Cook, P. F., and Uyeda, K.: Glutamate 325 Is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase. Biochemistry 39, 16238-16243.(2000).

(133) Karsten, W. E., Izumi, Y., and Cook, P. F.: Kinetic Mechanism of the Serine-Glyoxalate Aminotransferase from Holomicrobium methylovorum GM2. Arch. Biochem. Biophys. In Press (2001).

Books Authored/Edited

Enzyme Mechanism from Isotope Effects, Cook, P. F., Ed., CRC Press, Inc. Boca Raton, 1991.

Book Chapters

(1)  Cook, P. F. and Bertagnolli, B. L.  "Kinetics of Pyridine Nucleotide Utilizing Enzymes, " in Pyridine Nucleotide Coenzymes: Chemical, Biochemical and Medical Aspects, Vol. IIA, Chap. 12, Dolphin, D., Poulson, R. and Avramovic, O., Eds., John Wiley and Sons, Inc., New York, pp. 405-447, 1987.

(2)  Cook, P. F.  "Kinetic and Regulatory Mechanisms from Isotope Effects," in Enzyme Mechanism from Isotope Effects, Chap. 7, Cook, P. F., Ed., CRC Press, Inc. Boca Raton, 203-230, 1991.

(3)  Cook, P. F.  "pH Dependence of Isotope Effects," in Enzyme Mechanism from Isotope Effects, Chap. 8, Cook, P. F., Ed., CRC Press, Inc. Boca Raton, pp. 231-245, 1991.

(4)  Cook, P. F., Cho, Y.-K., and Mallick, S.  "Isotope Effects in Transferase Reactions," in Enzyme Mechanism from Isotope Effects, Chap. 17, Cook, P. F., Ed., CRC Press, Inc. Boca Raton, pp. 419-430, 1991.

(5)  Cook, P. F.  " Heavy Atom Isotope Effects in Enzyme-Catalyzed Reactions," in Isotopes in Organic Chemistry, Buncel, E., and Saunders, W. H., Eds., Elsevier, Amsterdam, pp. 69-132, 1992.

(6)  Jung, S., Hoffmann, R., Treptau, T., Rodriguez, P. H., Harris, B. G., Cook, P. F., and Hofer, H. W.  “Interaction of Protein Kinase AC from Ascaris suum with Proteins and Peptides:  Comparison with the Mammalian Enzyme” in Interacting Protein Domains:  Their Role in Signal and Energy Transduction, Nato ASI Series, Vol. H102, Heilmeyer, L., Ed., Springer Verlag, pp. 19-24, 1997.

(7) Tai, C.-H., and Cook, P. F.: Mechanism of the b-Replacement Reaction Catalyzed by O-Acetylserine Sulfhydrylase. Adv. Enzymol. Related Areas Mol. Biol. 74, 185-234, 2000.

Chapters in Symposium Volumes

(1)  Benjamin, R. C., Cook, P. F. and Jacobson, M. K.  "Kinetic Mechanism of Poly(ADP-Ribose) Polymerase," in Proceedings of the 7th International Symposium on ADP-Ribosylation Reactions, Hilz, H., and Shall, F., Eds., Springer Verlag, New York, pp. 93-97, 1985.

(2)  Cook, P. F., Nalabolu, S. R., and Tai, C.-H.  "Mechanism of the Beta-Replacement Enzyme, O-Acetylserine Sulfhydrylase," in Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds as Cofactors (Proceedings of the 8th International Symposium on Vitamin B6 and Carbonyl Catalysis, Fukui, T., Kagamiyama, H., Soda, K., and Wada, H., Eds., Pergamon Press, Tokyo, pp. 321-323, 1991.

(3)  Thomassin, H., Lagueux, J., Menard, L., Kirkland, J., Hengartner, C., Cook, P. F., and Poirier, G. G.  "Enzymatic Properties of poly(ADP-ribose)-Polymerase and poly(ADP-ribose)-Glycohydrolase on Chromatin," in ADP-Ribosylation Reactions, Poirier, G. G., and Moreau, P., Eds., Springer Verlag, New York, pp. 312-315, 1992.

(4)  Schnackerz, K. D., Podschun, B., and Cook, P. F.:  “Degradation of 5-Fluorouracil via the Pyrimidine Degradative Pathway” in Molecular Oncology and Clinical Applications, Cittadini, A., Baserga, R., Pinedo, H., Corda, D., and Galeotti, T., Eds., Birkhauser Verlag, Basel, pp. 347-352, 1993.

(5)  Schnackerz, K. D., Podschun, B., Jahnke, K., and Cook, P. F.:  “Kinetic Mechanism of Dihydropyrimidine Dehydrogenase:  An Iron-Sulfur Containing Enzyme” in Modern Enzymology:  Problems and Trends, Kurgsanov, B. I., Kochetkov, S. N., & Tishkov, V. I., Eds., Nova Science Publishers, Inc., Commack, pp. 473-480, 1994.

(6)  Schnackerz, K. D., and Cook, P. F.  "The Mechanism of O-Acetylserine Sulfhydrylase from Salmonella typhimurium" in Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds as Cofactors (Proceedings of the 9th International Symposium on Vitamin B6 and Carbonyl Catalysis, Marino, G., Sannia, G., and Bossa, F., Eds. Birkhäuser Verlag, Basel, pp. 205-209, 1994.

(7) Cook, P. F., Jansonius, J. N., and Burkhard, P.: “O-Acetylserine Sulfhydrylase: Mechanism of the a,b-Elimination Reaction” in Steenbock Symposium on Enzymatic Mechanisms, Frey, P. A. and Northrop, D. B., Eds. IOS Press, Amsterdam, pp. 204-214, 1999.

(8) Tai, C.-H., Burkhard, P., Jansonius, J. N., and Cook, P. F.: “Inhibition and Structural changes of O-Acetylserine Sulfhydrylase from Salmonella typhimurium Upon Binding Sulfate and Chloride Anions” in Biochemistry and Molecular Biology of Vitamin B6 and PQQ-Dependent Enzymes (Proceedings of the 10th International Symposium on Vitamin B6 and Carbonyl Catalysis), Iriarte, A., Kagan, H. M., and Martinez-Carrion, M., Eds. pp. 271-276, 2000.