163.  F. Wu, W.-S. Li, M. Chen-Goodspeed, M. Sogorb, and F. M. Raushel, “Rationally Engineered Mutants of Phosphotriesterase for Preparative Scale Isolation of Chiral Organophosphates” Journal of American Chemical Society 122, 10206-10207 (2000).

 

162.  M. M. Benning, S. B. Hong, F. M. Raushel and H. M. Holden, “The Binding of Substrate Analogs to Phosphotriesterase” Journal of Biological Chemistry 275, 30546-30550 (2000).

161.  W. Zhu, W.-S. Li, F. M. Raushel, and G. Vigh, “Experimental Verification of a Predicted, Hitherto Unseen Separation Selectivity Pattern in the Capillary Electrophoretic Separation of Nonchared Enantiomers by Octakis(2,3-Diacetyl-6-Sulfato)-g-Cylclodextrin” Electrophoresis 21, 3249-3256 (2000).

160.  W. Zhu, F. Wu, F. M. Raushel, and G. Vigh, “Capillary Electrophoretic Separation of the Enantiomers of Organophosphates with a Phosphorus Stereogenic Center Using Octakis(2,3-diacetyl-6-sulfato)-g-cyclodextrinas Resolving Agent” Journal of Chromatography 895, 247-254 (2000).

159.  X. Huang and F. M. Raushel, “Restricted Passage of Reaction Intermediates Through the Ammonia Tunnel of Carbamoyl Phosphate Synthetase” Journal of Biological Chemistry 275, 26233-26240 (2000).

158.  X. Huang and F. M. Raushel, “Role of the Hinge Loop Linking the N- and C-Terminal Domains of the Amidotransferase Subunit of Carbamoyl Phosphate Synthetase” Archives of Biochemistry and Biophysics 380, 174-180 (2000).

157.  Healy, V. L., Mullins, L. S., Li, X., Hall, S. E., Raushel, F. M. and Walsh, C. T. “D-Ala-D-XLigases: Evaluation of D-Alanyl Phosphate Intermediate by MIX, PIX and Rapid Quench Studies” Chemistry and Biology 7, 505-514 (2000).

156.  C. Hill, F. Wu, T. Chen., J. DeFrank, and F. M. Raushel, “Substrate and Stereochemical Specificity of the Organophosphorus Acid Anhydrolase from Alteromonas sp. JD6.5 Toward p-Nitrophenyl Phosphotriesters" Bioorganic and Medicinal Chemistry Letters, 10, 1285-1288. (2000).

155.  H. Shim and F. M. Raushel, “Self-Assembly of the Binuclear Metal Center of Phosphotriesterase” Biochemistry 39, 7357-7364 (2000).

 

154.  B. W. Miles and F. M. Raushel, “Synchronization of the Three Reaction Centers within Carbamoyl Phosphate Synthetase” Biochemistry 39, 5051-5056 (2000).

153.  F. M. Raushel and H. M. Holden, “Phosphotriesterase: An Enzyme in Search of Its Natural Substrate” Advances in Enzymology 74, 51-93 (2000).

152.   X. Huang and F. M. Raushel, “An Engineered Blockage within the Ammonia Tunnel in Carbamoyl Phosphate Synthetase Prevents of the Use of Glutamine as a Substrate but not Ammonia” Biochemistry 39, 3240-3247 (2000).

151.  F. Javid-Majd, L. S. Mullins, F. M. Raushel, and M. A. Stapleton, “The Differentially Conserved Residues of Carbamoyl Phosphate Synthetase” Journal of Biological Chemistry 275, 5073-5080 (2000).

150.  H. M. Holden, F. M. Raushel, and J. B. Thoden, “Carbamoyl Phosphate Synthetase: An Amazing Biochemical Odyssey from Substrate to Product” Cellular and Molecular Life Sciences 56, 507-522 (1999).

149.  J. B. Thoden, X. Huang, F. M. Raushel, and H. M. Holden, “The Small Subunit of Carbamoyl Phosphate Synthetase: Snapshots Along the Reaction Pathway” Biochemistry 38, 16158-16166 (1999).

148.  X. Huang and F. M. Raushel, “Deconstruction of the Catalytic Array within the Amidotransferase Subunit of Carbamoyl Phosphate Synthetase” Biochemistry 38, 15909-15914 (1999).

147.  M. Chen-Goodspeed, J. Vanhooke, H. M. Holden, and F. M. Raushel, “Kinetic Mechanism of Kanamycin Nucleotidyltransferase from Stapylococcus aureus” Bioorganic Chemistry 27, 395-408 (1999).

146.  S.-B. Hong and F. M. Raushel, “Stereochemical Constraints on the Catalytic Hydrolysis of Organosphosphate Nerve Agents by Phosphotriesterase” Phosphorus, Sulfur, and Silicon and the Related Elements, 144, 521-524 (1999).

145.  J. B Thoden, F. M. Raushel, G. Wesenburg, and H. M. Holden, “The Binding of Inosine Monophosphate to E. coli Carbamoyl Phosphate Synthetase” Journal of Biological Chemistry 274, 22502-22507 (1999).

 

144.   K. Tuovinen, E. Kaliste-Korhonen, F. M. Raushel, and O. Hanninen, “Success of Pyridostigmine, Physostigmine, Eptastigmine and Phosphotriesterase Treatments in Acute Sarin Intoxication” Toxicology 134, 169-178 (1999).

143.  T. O. Baldwin, M. M. Zeigler, and F. M. Raushel, “Structure, Folding, and Mechanism of Bacterial Luciferase", in Bioluminescence and Chemiluminescence: Perspective for the 21st Centrury. (Roda, K. A., Pazzagli, M., Kricka, L. J. and Stanley, P. E., eds.) John Wiley & Sons, England pp. 376-379 (1999).     

142.  S. B. Hong and F. M. Raushel, “Stereochemical Preferences for Chiral Substrates by the Bacterial Phosphotriesterase” Chemico-Biological Interactions 119, 225-234 (1999).

141.  F. M. Raushel, J. B. Thoden, and H. M. Holden, “The Amidotransferase Family of Enzymes:  Molecular Machines for the Production and Delivery of Ammonia” Biochemistry 38, 7891-7899 (1999).

140.  L. M. Mullins and F. M. Raushel, “Channeling of Ammonia Through the Intermolecular Tunnel Contained within Carbamoyl Phosphate Synthetase” Journal of American Chemical Society 121, 3803-3804 (1999).

139.  J. B. Thoden, G. Wesenberg, F. M. Raushel, and H. M. Holden, “Carbamoyl Phosphate Synthetase: Closure of the B-domain as a Result of Nucleotide Binding” Biochemistry 38, 2347-2357 (1999).

138.  F. M. Raushel, L. S. Mullins, and G. Gibson, “Detection of Intermediates in the Carbamoyl Phosphate Synthetase Reaction” in Enzyme Mechanisms  (P. A. Frey and D. B. Northrop, eds.) IOS Press, Amsterdam, Netherlands pp. 61-71 (1999).

137.  B. L. Braxton, L. S. Mullins, F. M. Raushel, G. D. Reinhart, “Allosteric Dominance in Carbamoyl Phosphate Synthetase” Biochemistry 38, 1394-1401 (1999).

136.  S.-B Hong and F. M. Raushel, “Stereochemical Constraints on the Substrate Specificity of Phosphotriesterase” Biochemistry 38, 1159-1165 (1999).     

135.  J. B. Thoden, F. M. Raushel, M. M. Benning, I. Rayment, and H. M. Holden, “The Structure of Carbamoyl Phosphate Synthetase Determined to 2.1 Å Resolution” Acta Crystallographica, Part D 55, 8-24 (1999).

134.  H. M. Holden, J. B. Thoden, and F. M. Raushel, “Carbamoyl Phosphate Synthetase: A Tunnel Runs Through It” Current Opinion in Structural Biology 8, 679-685 (1998).

133.  G. W. Gibson, L. S. Mullins, and F. M. Raushel, “Carbamoyl Phosphate Synthetase from Escherichia coli does not Catalyze the Dehydration of Bicarbonate to Carbon Dioxide", Bioorganic Chemistry 26, 255-268 (1998).      

132.  B. W. Miles, J. A. Banzon, and F. M. Raushel, “Regulatory Control of the Amidotransferase Domain of Carbamoyl Phosphate Synthetase” Biochemistry 37, 16773-16779 (1998).

131.  F. M. Raushel, J. B. Thoden, G. D. Reinhart, and H. M. Holden, “Carbamoyl Phosphate Synthetase: A Crooked Path from Substrates to Products” Current Opinion in Chemical Biology 2, 624-632 (1998).

130.  F. M. Raushel, L. S. Mullins, and G. E. Gibson, “A Stringent Test for the Nucleotide Switch Mechanism of Carbamoyl Phosphate Synthetase” Biochemistry 37, 10272-10278 (1998).

129.  H. Shim, S. B. Hong and F. M. Raushel, “Hydrolysis of Phosphodiesters through Transformation of the Bacterial Phosphotriesterase” Journal of Biological Chemistry 273, 17445-17450 (1998).

128.  J. B. Thoden, S. G. Miran, J. C. Phillips, A J. Howard, F. M. Raushel, and H. M. Holden, "Carbamoyl Phosphate Synthetase: Caught in the Act of Glutamine Hydrolysis” Biochemistry 37, 8825-8831 (1998).

127.  W. A. Francisco, H. M. Abu-Soud, A. J. DelMonte, D. A. Singleton, T. O. Baldwin, and F. M. Raushel, “Deuterium Kinetic Isotope Effect and the Mechanism of the Bacterial Luciferase Reaction” Biochemistry 37, 2596-2606 (1998).

126.  L. M. Watkins, J. M. Kuo, M. Chen-Goodspeed and F. M. Raushel, “A Combinatorial Library for the Binuclear Metal Center of Bacterial Phosphotriesterase” PROTEINS: Structure, Function and Genetics 29, 553-561 (1997).

125.  T. O. Baldwin, M. M. Ziegler, A. C. Clark, J. F. Sinclair, F. M. Raushel, I. Rayment, H. M. Holden, A. J. Fisher, T. B. Thompson, and J. B. Thoden, “Structure and Folding of Bacterial Luciferase” in Flavins and Flavoproteins (1996) (K. J. Stevenson, V. Massey and C. H. Williams, eds) University of Calgary Press, pp. 347-356 (1997).

124.  L. M. Watkins, H. J. Mahoney, J. K. McCulloch, and F. M. Raushel, “Augmented Hydrolysis of DFP in Engineered Mutants of Phosphotriesterase” Journal of Biological Chemistry 272, 25596-25627 (1997).

123.  S. B. Hong and F. M. Raushel, “Inhibitors Directed Towards the Binuclear Metal Center of Phosphotriesterase” Journal of Enzyme Inhibition 12, 191-203 (1997).

122.  L. S. Mullins, C. N. Pace, and F. M. Raushel, “Conformational Stability of Ribonuclease T1 Determined by Hydrogen-Deuterium Exchange” Protein Science 6, 1387-1395 (1997). PMCID: PMC2143755

 

121.  H. M. Abu-Soud, R. Batchui, F. M. Raushel, D. J. Stuehr, “The Ferrous-dioxy Complex of Neuronal Nitric-oxide Synthase” Journal of Biological Chemistry 272, 17349-17353 (1997).

120.  L. S. Mullins, S. B. Hong, G. E. Gibson, H. Walker, T. C. Stadtman, and F. M. Raushel, “Identification of a Phosphorylated Enzyme Intermediate in the Catalytic Mechanism for Selenophosphate Synthetase” Journal of American Chemical Society 119, 6684-6685 (1997).

 

119.  S. B. Hong, L. S. Mullins, H. Shim, and F. M. Raushel, “Mechanism-Based Inhibitors for the Inactivation of the Bacterial Phosphotriesterase” Biochemistry 36, 9022-9028 (1997).

118.  J. B. Thoden, H. M. Holden, G. Wesenberg, F. M. Raushel, and I. Rayment, “The Structure of Carbamoyl Phosphate Synthetase: A Journey of 96 Å from Substrate to Product” Biochemistry 36, 6305-6316 (1997).

 117.  J. M. Kuo, M. Y. Chae, and F. M. Raushel, “Perturbations to the Active Site of Phosphotriesterase” Biochemistry 36, 1982-1988 (1997).

116.  K. Tuovinen, E. Kaliste-Korhonen, F. M. Raushel, and O. Hanninen, “Phosphotriesterase, Pralidoxime-2-Chloride (2-PAM) and Eptastigmine Treatments and Their Combinations in DFP Intoxication” Toxicology and Applied Pharmacology 141, 555-560 (1996).

115.  K. Tuovinen, E. Kaliste-Korhonen, F. M. Raushel, and O. Hanninen, “Eptastigmine-Phosphotriesterase Combination in DFP Intoxication” Toxicology and Applied Pharmacology 140, 364-369 (1996).

114.  F. Javid-Majd, M. A. Stapleton, M. F. Harmon, B. A. Hanks, L. S. Mullins, and F. M. Raushel, “Comparison of the Functional Differences for the Homologous Residues Within the Carboxy Phosphate and Carbamate Domains of Carbamoyl Phosphate Synthetase” Biochemistry 35, 14362-14369 (1996).

 

113.  M. A. Stapleton, F. Javid-Majd, M. F. Harmon, B. A. Hanks, J. L. Grahmann, L. S. Mullins, and F. M. Raushel, “Role of Conserved Residues Within the Carboxy Phosphate Domain of Carbamoyl Phosphate Synthetase” Biochemistry 35, 14352-14361 (1996).

 

112.  L. C. Lo, C. H. Lo, K. D. Janda, D. B. Kassel, and F. M. Raushel,  “A Versatile Mechanism Based Reaction Probe for the Direct Selection of Biocatalysts”  Bioorganic and Medicinal Chemistry Letters, 6, 2117-2120 (1996).

111.  B. L. Braxton, L. S. Mullins, F. M. Raushel, and G. D. Reinhart, “The Allosteric Effects of Carbamoyl Phosphate Synthetase from E. coli are Entropy-Driven” Biochemistry 35, 11918-11924 (1996).

110.  S.-B. Hong and F. M. Raushel, “Metal-Substrate Interactions Facilitate the Catalytic Activity of the Bacterial Phosphotriesterase” Biochemistry 35, 10904-10912 (1996).

           

109.  J. L. Johnson and F. M. Raushel, “The Influence of Primary Sequence Transpositions on the Folding Pathways of Ribonuclease T1” Biochemistry 35, 10223-10233 (1996).

 

108.  K. Tuovinen, E. Kaliste-Korhonen, F. Raushel, and O. Hanninen, “Protection of Organophosphate-Inactivated Esterases with Phosphotriesterase” Fundamental & Applied Pharmacology 31, 210-217 (1996).

107.  J. L. Vanhooke, M. M. Benning, F. M. Raushel, and H. M. Holden, “Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with the Bound Substrate Analog Diethyl 4-Methylbenzylphosphonate” Biochemistry 35, 6020-6025 (1996).

106.  J. B. Garrett, L. S. Mullins, and F. M. Raushel, “Are Turns Required for the Folding of Ribonuclease T1” Protein Science 5, 204-211 (1996). PMCID: PMC2143342

105.  W. A. Francisco, H. M. Abu-Soud, R. Topgi, T. O. Baldwin, and F. M. Raushel, “Interaction of Bacterial Luciferase with 8-Substituted Flavin Mononucleotide Derivatives” Journal of Biological Chemistry 271, 104-110 (1996).