Click here for Michael Toney's mini-CV

Click here to run a PubMed search for Michael Toney's publications

Click on any highlighted title below to open the article PDF

1.         Hill, M.P., et al., Rapid photodynamics of vitamin B6 coenzyme pyridoxal 5'-phosphate and its Schiff bases in solution. J Phys Chem B, 2008. 112(18): p. 5867-73.

2.         Spies, M.A. and M.D. Toney, Intrinsic primary and secondary hydrogen kinetic isotope effects for alanine racemase from global analysis of progress curves. J Am Chem Soc, 2007. 129(35): p. 10678-85.

3.         Sharif, S., et al., Coupling of functional hydrogen bonds in pyridoxal-5'-phosphate-enzyme model systems observed by solid-state NMR spectroscopy. J Am Chem Soc, 2007. 129(14): p. 4440-55.

4.         Sharif, S., et al., 15N nuclear magnetic resonance studies of acid-base properties of pyridoxal-5'-phosphate aldimines in aqueous solution. J Phys Chem B, 2007. 111(15): p. 3869-76.

5.         Sharif, S., et al., NMR localization of protons in critical enzyme hydrogen bonds. J Am Chem Soc, 2007. 129(31): p. 9558-9.

6.         Sharif, S., et al., NMR studies of coupled low- and high-barrier hydrogen bonds in pyridoxal-5'-phosphate model systems in polar solution. J Am Chem Soc, 2007. 129(19): p. 6313-27.

7.         Sharif, S., et al., X-ray crystallographic structures of enamine and amine Schiff bases of pyridoxal and its 1:1 hydrogen-bonded complexes with benzoic acid derivatives: evidence for coupled inter- and intramolecular proton transfer. Acta Crystallogr B, 2006. 62(Pt 3): p. 480-7.

8.         Sharif, S., et al., NMR studies of solvent-assisted proton transfer in a biologically relevant Schiff base: toward a distinction of geometric and equilibrium H-bond isotope effects. J Am Chem Soc, 2006. 128(10): p. 3375-87.

9.         Schnackerz, K.D., et al., Ionization state of pyridoxal 5'-phosphate in D-serine dehydratase, dialkylglycine decarboxylase and tyrosine phenol-lyase and the influence of monovalent cations as inferred by 31P NMR spectroscopy. Biochim Biophys Acta, 2006. 1764(2): p. 230-8.

10.       He, Z. and M.D. Toney, Direct detection and kinetic analysis of covalent intermediate formation in the 4-amino-4-deoxychorismate synthase catalyzed reaction. Biochemistry, 2006. 45(15): p. 5019-28.

11.       Dixon, S.M., et al., Slow-binding human serine racemase inhibitors from high-throughput screening of combinatorial libraries. J Med Chem, 2006. 49(8): p. 2388-97.

12.       Dixon, S., et al., Aminodeoxychorismate synthase inhibitors from one-bead one-compound combinatorial libraries: "staged" inhibitor design. J Med Chem, 2006. 49(25): p. 7413-26.

13.       Toney, M.D., Reaction specificity in pyridoxal phosphate enzymes. Arch Biochem Biophys, 2005. 433(1): p. 279-87.

14.       Liu, W., et al., Kinetic and crystallographic analysis of active site mutants of Escherichia coli gamma-aminobutyrate aminotransferase. Biochemistry, 2005. 44(8): p. 2982-92.

15.       Foltyn, V.N., et al., Serine racemase modulates intracellular D-serine levels through an alpha,beta-elimination activity. J Biol Chem, 2005. 280(3): p. 1754-63.

16.       Fogle, E.J., et al., Role of Q52 in catalysis of decarboxylation and transamination in dialkylglycine decarboxylase. Biochemistry, 2005. 44(50): p. 16392-404.

17.       Tu, S.L., et al., Biliverdin reduction by cyanobacterial phycocyanobilin:ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates. J Am Chem Soc, 2004. 126(28): p. 8682-93.

18.       Spies, M.A., et al., Alanine racemase free energy profiles from global analyses of progress curves. J Am Chem Soc, 2004. 126(24): p. 7464-75.

19.       Liu, W. and M.D. Toney, Kinetic and thermodynamic analysis of the interaction of cations with dialkylglycine decarboxylase. Biochemistry, 2004. 43(17): p. 4998-5010.

20.       Liu, W., et al., Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gamma-aminobutyrate aminotransferase. Biochemistry, 2004. 43(34): p. 10896-905.

21.       He, Z., et al., Conservation of mechanism in three chorismate-utilizing enzymes. J Am Chem Soc, 2004. 126(8): p. 2378-85.

22.       Zhou, X., R. Medhekar, and M.D. Toney, A continuous-flow system for high-precision kinetics using small volumes. Anal Chem, 2003. 75(15): p. 3681-7.

23.       Spies, M.A. and M.D. Toney, Multiple hydrogen kinetic isotope effects for enzymes catalyzing exchange with solvent: application to alanine racemase. Biochemistry, 2003. 42(17): p. 5099-107.

24.       Christenson, S.D., et al., Kinetic analysis of the 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis. Biochemistry, 2003. 42(43): p. 12708-18.

25.       Christenson, S.D., et al., A novel 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis. J Am Chem Soc, 2003. 125(20): p. 6062-3.

26.       Liu, W., et al., Aminophosphonate inhibitors of dialkylglycine decarboxylase: structural basis for slow binding inhibition. Biochemistry, 2002. 41(41): p. 12320-8.

27.       Zhou, X., et al., Rapid kinetic and isotopic studies on dialkylglycine decarboxylase. Biochemistry, 2001. 40(5): p. 1367-77.

28.       Zabinski, R.F. and M.D. Toney, Metal ion inhibition of nonenzymatic pyridoxal phosphate catalyzed decarboxylation and transamination. J Am Chem Soc, 2001. 123(2): p. 193-8.

29.       Toney, M.D., Computational studies on nonenzymatic and enzymatic pyridoxal phosphate catalyzed decarboxylations of 2-aminoisobutyrate. Biochemistry, 2001. 40(5): p. 1378-84.

30.       Sanchez, C., et al., Cloning and characterization of a phosphopantetheinyl transferase from Streptomyces verticillus ATCC15003, the producer of the hybrid peptide-polyketide antitumor drug bleomycin. Chem Biol, 2001. 8(7): p. 725-38.

31.       Zhou, X. and M.D. Toney, pH studies on the mechanism of the pyridoxal phosphate-dependent dialkylglycine decarboxylase. Biochemistry, 1999. 38(1): p. 311-20.

32.       Sun, S. and M.D. Toney, Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase. Biochemistry, 1999. 38(13): p. 4058-65.

33.       Malashkevich, V.N., et al., Crystal structures of dialkylglycine decarboxylase inhibitor complexes. J Mol Biol, 1999. 294(1): p. 193-200.

34.       Zhou, X., S. Kay, and M.D. Toney, Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ions. Biochemistry, 1998. 37(16): p. 5761-9.

35.       Sun, S., R.F. Zabinski, and M.D. Toney, Reactions of alternate substrates demonstrate stereoelectronic control of reactivity in dialkylglycine decarboxylase. Biochemistry, 1998. 37(11): p. 3865-75.

36.       Sun, S., C.K. Bagdassarian, and M.D. Toney, Pre-steady-state kinetic analysis of the reactions of alternate substrates with dialkylglycine decarboxylase. Biochemistry, 1998. 37(11): p. 3876-85.

37.       Toney, M.D., S. Pascarella, and D. De Biase, Active site model for gamma-aminobutyrate aminotransferase explains substrate specificity and inhibitor reactivities. Protein Sci, 1995. 4(11): p. 2366-74.

38.       Toney, M.D., et al., Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase. J Mol Biol, 1995. 245(2): p. 151-79.

39.       Toney, M.D. and J.F. Kirsch, Lysine 258 in aspartate aminotransferase: enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift. Biochemistry, 1993. 32(6): p. 1471-9.

40.       Toney, M.D., et al., Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites. Science, 1993. 261(5122): p. 756-9.

41.       Malashkevich, V.N., M.D. Toney, and J.N. Jansonius, Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase. Biochemistry, 1993. 32(49): p. 13451-62.

42.       Toney, M.D. and J.F. Kirsch, Bronsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant. Protein Sci, 1992. 1(1): p. 107-19.

43.       Toney, M.D. and J.F. Kirsch, Tyrosine 70 fine-tunes the catalytic efficiency of aspartate aminotransferase. Biochemistry, 1991. 30(30): p. 7456-61.

44.       Toney, M.D. and J.F. Kirsch, Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase. Biochemistry, 1991. 30(30): p. 7461-6.

45.       Toney, M.D. and J.F. Kirsch, The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate. J Biol Chem, 1991. 266(35): p. 23900-3.

46.       Toney, M.D., et al., Crystallization and preliminary X-ray diffraction studies of dialkylglycine decarboxylase, a decarboxylating transaminase. J Mol Biol, 1991. 222(4): p. 873-5.

47.       Kirsch, J.F. and M.D. Toney, Bronsted analysis of enzymatic proton transfer reactions through site-directed mutagenesis. Ann N Y Acad Sci, 1990. 585: p. 48-57.

48.       Toney, M.D. and J.F. Kirsch, Direct Bronsted analysis of the restoration of activity to a mutant enzyme by exogenous amines. Science, 1989. 243(4897): p. 1485-8.

49.       Smith, D.L., et al., 2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli. Biochemistry, 1989. 28(20): p. 8161-7.

50.       Julin, D.A., et al., Estimation of free energy barriers in the cytoplasmic and mitochondrial aspartate aminotransferase reactions probed by hydrogen-exchange kinetics of C alpha-labeled amino acids with solvent. Biochemistry, 1989. 28(9): p. 3815-21.

51.       Toney, M.D. and J.F. Kirsch, Tyrosine 70 increases the coenzyme affinity of aspartate aminotransferase. A site-directed mutagenesis study. J Biol Chem, 1987. 262(26): p. 12403-5.