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• Kurz, L.C., Constantine, C.Z., Jiang, H. and Kappock, T.J. The partial substrate dethiaacetyl-coenzyme A mimics all critical carbon acid reactions in the condensation half-reaction catalyzed by thermoplasma acidophilum citrate synthase. Biochemistry 48:7878-7891 (2009).
• Kurz, L.C., Fite, B., Jean, J., Park, J., Erpelding, T. and Callis, P. Photophysics of tryptophan fluorescence: Link with the catalytic strategy of the citrate synthase from Thermoplasma acidophilum. Biochem 44:1394-1413 (2005).
• Kurz, L.C., Drysdale, G., Riley, M., Tomar, M.A., Chen, J., Russell, R.J.M. and Danson, M.J. Kinetics and Mechanism of the Citrate Synthase from the Thermophilic Archaeon, Thermoplasma acidophilum, Biochemistry 39:2283-2296 (2000).
• Gu, Z., Drueckhammer, D.G., Kurz, L., Liu, K., Martin, D.P., and McDermott, A. Mechanism of Condensation Reaction of Citrate Synthase as Studied by Solid State NMR: Protonation States and Hydrogen Bonding Environment in the Binding Site of Acetylcoenzyme A Analog-Citrate Synthase Complexes. Biochemistry 38:8022-8031 (1999).
• Deng, H., L.C. Kurz, et al. Characterization of hydrogen bonding in the complex of adenosine deaminase with transition state analogue: a Raman spectroscopic study. Biochemistry 37:4968-4976 (1998).
• Kurz, L.C., T. Nakra, et al. Effects of changes in three catalytic residues on the relative stabilities of some of the intermediates and transition states in the citrate synthase reaction. Biochemistry 37:9724-9737 (1998).
• Kurz, L. C., Roble, J.H., Nakra, T., et al. Ability of single-site mutants of citrate synthase to catalyze proton transfer from the methyl group of dethiaacetyl-coenzyme A, a non-thioester substrate analog. Biochemistry 36:3981-3990 (1997).
• Evans, C. T., Kurz, L.C., Remington, S. J., and Srere, P. A. Active site mutants of pig citrate synthase: effects of mutations on the enzyme catalytic and structural properties. Biochemistry 35:10661-10672 (1996).
• Mohamedali, K. A., Kurz, L. C., and Rudolph, F. B. Site-directed mutagenesis of active site glutamate-217 in mouse adenosine deaminase. Biochemistry 35:1672-1680 (1996).
• Sideraki, V., Wilson, D. K., Kurz, L. C., Quiocho, F. A., and Rodolph, F. B. Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation. Biochemistry 35:15019-15208 (1996).
• Kurz, L. C., Shah, S., Frieden, C., et al. Catalytic strategy of citrate synthase: subunit interactions revealed as a consequence of a single amino acid change in the oxaloacetate binding site. Biochemistry 34:13278-13288 (1995).