(1970 – present)
1. Stereoselective Decomposition of an Octahedral Complex During Bacterial Growth; Gillard, R. D., and Thorpe, C. (1970) Chemical Communications, 997-998.
2. Resolution of 1,2,3-Triglycinatocobalt(III) by a Bacterial Method and Determination of its Optical Purity by Isotope Dilution; Gillard, R. D., Lyons, J. R., and Thorpe, C. (1972) J. Chem. Soc. Dalton, 1584-1586.
3. Ph.D. Thesis: Stereoselective Interactions of Cobalt Complexes with Bacteria (1972) University of Kent at Canterbury.
4. Stereoselective Reduction of Cobalt(III) Complexes by Bacteria; Thorpe, C., and Gillard, R. D. (1975) Biochem. Biophys. Acta 392, 175-183.
5. Effects of Low Concentrations of Guanidine Hydrochloride on Pig Heart Lipoamide Dehydrogenase; Thorpe, C., and Williams, C. H. (1974) Biochemistry 13, 3263-3267.
6. Modification of Pig Heart Lipoamide Dehydrogenase by Cupric Ions; Thorpe, C., and Williams, C. H. (1975) Biochemistry 14, 2419-2423.
7. Differential Reactivity of the Two Active Site Cysteine Residues Generated on Reduction of Pig Heart Lipoamide Dehydrogenase; Thorpe, C., and Williams, C. H. (1976) J. Biol. Chem. 251, 3553-3557.
8. Spectral Evidence for a Flavin Adduct in a Monoalkylated Derivative of Pig Heart Lipoamide Dehydrogenase; Thorpe, C., and Williams, C. H. (1976) J. Biol. Chem. 251, 7726-7728.
9. Ion Pair Formation in Pig Heart Lipoamide Dehydrogenase. Rationalization of pH-profiles for Reactivity of Oxidized Enzyme with Dihydrolipoamide and 2-electron Reduced Enzyme and Lipoamide and Iodoacetamide; Matthews, R. G., Ballou, D. P., Thorpe, C., and Williams, C. H. (1977). J. Biol. Chem. 252, 3199-3207.
10. Functional Roles of the Two Active Site Cysteine Residues Generated on Reduction of Lipoamide Dehydrogenase and Glutathione Reductase; Mechanisms of Oxidizing Enzymes, Williams, C. H., Thorpe, C., and Arscott, L. D. (1978) (Singer, T. P., Ondarza, R., eds.) pp. 3-16, Elsevier.
11. An Acyl-CoA Dehydrogenase from Pig Kidney: Purification and Properties; Thorpe, C., Matthews, R. G., and Williams, C. H. (1979) Biochemistry 18, 331-337.
12. Purification and Some Properties of an Acyl-CoA Dehydrogenase from Pig Kidney, Flavins, and Flavoproteins; Thorpe, C., Matthews, R. G., and Williams, C. H. (Yagi, K., and Yamano, T., eds.) (1980) pp. 209-216, Japan Scientific Societies Press.
13. An Essential Methionine in Pig Kidney General Acyl-CoA Dehydrogenase; Mizzer, J. P., and Thorpe, C. (1980) Biochemistry 19, 5500-5504.
14. Suicide Substrates as Irreversible Inhibitors of Flavoenzymes; Ghisla, S., Wenz, A., and Thorpe, C. (1980) (Brodbeck, U., ed.) “Enzyme Inhibitors,” Verlag Chemie, 43-60.
15. Methodology Employed for Anaerobic Spectrophotometric Titrations for Computer Assisted Analysis of the Data; Williams, C. H., Arscott, L. D., Matthews, R. G., Thorpe, C., and Wilkinson, K. D. (1980) Methods in Enzymology 62D, 185-198.
16. Lipoamide Dehydrogenase from Pig Heart-Pyridine Nucleotide Induced Changes in Monoalkylated Two-Electron-Reduced Enzyme; Thorpe, C., and Williams, C. H. (1981) Biochemistry 20, 1507-1515.
17. Glutathione Reductase from Yeast – Differential Reactivity of the Nascent Thiol in 2-Electron Reduced Enzyme and Properties of a Monoalkylated Derivative; Arscott, L. D., Thorpe, C., and Williams, C. H. (1981) Biochemistry 20, 1507-1515.
18. An Acyl-CoA Dehydrogenase from Pig Kidney, Thorpe, C. (1981) (Lowenstein, J. M., ed.) Methods in Enzymology 71, 366-374.
19. Interaction of Long Chain Acyl-CoA Analogs with Pig Kidney General Acyl-CoA Dehydrogenase; Thorpe, C., Ciardelli, T. L., Stewart, C. J., and Wieland, Th. (1981) Eur. J. Biochem. 118, 179-182.
20. Stabilization of the Red Semiquinone Form of Pig Kidney General Acyl-CoA Dehydrogenase by Acyl-CoA Derivatives; Mizzer, J. P., and Thorpe (1981) Biochemistry 19, 4965-4970.
21. A Method for the Resolution of General Acyl-CoA Dehydrogenase Apoprotein, Mayer, E. J., and Thorpe, C. (1981) Anal. Biochem. 116, 227-229.
22. Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A.; Wenz, A., Thorpe, C., and Ghisla, S. (1981) J. Biol. Chem. 256, 9809-9812.
23. Reaction of General Acyl-CoA Dehydrogenase with 3,4-Pentadienoyl-CoA; Wenz, A., Ghisla, S., and Thorpe, C. (1981) in Flavins and Flavoproteins (V. Massey and C. H. Williams, Jr., eds.) Elsevier North Holland, N.Y., pp. 605-608.
24. Stabilization of the Red Semiquinone Form of General Acyl-CoA Dehydrogenase by Acyl-CoA Derivatives; Mizzer, J. P., and Thorpe, C. (1981) in Flavins and Flavoproteins (V. Massey and C. H. Williams, Jr., eds.) Elsevier North Holland, N.Y., 637-640.
25. Coenzyme A Persulfide, the Tightly-Bound Ligand in the Green Form of Butyryl-CoA Dehydrogenase; Williamson, G., Engel, P. C., Mizzer, J. P., Thorpe, C., and Massey, V. (1981) in Flavins and Flavoproteins (V. Massey and C. H. Williams, Jr., eds.) Elsevier North Holland, N.Y., 593-598.
26. Pig Kidney General Acyl-CoA Dehydrogenase: Flavin Analog Studies; Thorpe, C., and Massey, V. (1981) in Flavins and Flavoproteins (V. Massey and C. H. Williams, Jr., eds.) Elsevier North Holland, N.Y., 641-644.
27. Evidence that the Greening Ligand in Native Butyryl-CoA Dehydrogenase Is a CoA Persulfide; Williams, G., Engel, P. C., Mizzer, J. P., Thorpe, C., and Massey, V. (1982) J. Biol. Chem. 257, 4314-4320.
28. The Cyclic Voltammetry and Derivative Cyclic Voltabsorptometry of Purified Horse Heart Cytochrome c at Tin Doped Optically Transparent Electrodes; Bowden, E. F., Hawkridge, F. M., Cheblowski, J., Bancroft, E. E., Thorpe, C., and Blount, H. N. (1982) J. Amer. Chem. Soc. 104, 7641-7644.
29. Modification of an Arginine Residue in Pig Kidney General Acyl-CoA Dehydrogenase by 1,2-cyclohexanedione; Jiang, Z-y., and Thorpe, C., (1982) Biochem. J. 207, 415-419.
30. Purification and Properties of Pig Kidney Electron Transferring Flavoprotein; Gorelick, R. J., and Thorpe, C. (1982) Biochemistry 21, 6936-6942.
31. Flavin Analog Studies of Pig Kidney General Acyl-CoA Dehydrogenase; Thorpe, C., and Massey, V. (1983) Biochemistry 22, 2972-2978.
32. Yeast Acyl-CoA Oxidase: Purification and Properties; Jiang, Z-y., and Thorpe, C., and Massey, V. (1983) Biochemistry 22, 3752-3758.
33. Mechanistic Studies with General Acyl-CoA Dehydrogenase and Butyryl-CoA Dehydrogenase: Evidence for the Transfer of the -hydrogen to the Flavin N(5)-Position as a Hydride; Ghisla, S., Thorpe, C., and Massey, V. (1984) Biochemistry 23, 3154-3161.
34. The Influence of Oxidation-Reduction State on the Kinetic Stability of Pig Kidney General Acyl-CoA Dehydrogenase and Other Flavoproteins; Madden, M., Lau, S-Z., and Thorpe, C. (1984) Biochem. J. 224, 577-580.
35. Inactivation of Pig Kidney General Acyl-CoA Dehydrogenase by 2-Alkynoyl-CoA Derivatives; Freund, K., Mizzer, J. P., and Thorpe, C. (1984) in Flavins and Flavoproteins (Bray, R., Engel, P., and Mayhew, S., eds.) Walter de Gruyter, New York., pp. 443-446.
36. Flavin Analog Studies of Pig Kidney Electron-Transferring Flavoprotein; Gorelick, R. G., and Thorpe, C. (1984) in Flavins and Flavoproteins (Bray, R., Engel, P., and Mayhew, S., eds.) Walter de Gruyter, New York, pp. 761-764.
37. Studies with General Acyl-CoA Dehydrogenase from Pig Kidney: Inactivation by a Novel Type of Suicide Inhibitor, 3,4-pentadienoyl-CoA; Wenz, A., Ghisla, S., and Thorpe, C. (1985) Eur. J. Biochem. 147, 553 560.
38. Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by 2 Alkynoyl-CoA Derivatives; Initial Aspects; Freund, K., Mizzer, J. P., Dick, W., and Thorpe, C. (1985) Biochemistry 24, 5996-6002.
39. Interflavin Oxidation-Reduction Reactions Between Pig Kidney General Acyl-CoA Dehydrogenase and Electron Transferring Flavoprotein; Gorelick, R. J., Schopfer, L. M., Ballou, D. P., Massey, V., and Thorpe, C. (1985) Biochemistry 24, 6830-6839.
40. A Method for the Preparation of 3-Ketoacyl-CoA Derivatives; Thorpe, C. (1986) Analytical Biochemistry 155, 391-394.
41. Medium Chain Acyl-CoA Dehydrogenase from Pig Kidney has Intrinsic Enoyl-CoA Hydratase Activity. Lau, S-M., Powell, P., Buettner, H., Ghisla, S., and Thorpe, C. (1986) Biochemistry 25, 4184-4189.
42. Electron-Transferring Flavoprotein from Pig Kidney: Flavin Analog Studies; Gorelick, R. J., and Thorpe, C. (1986) Biochemistry 25, 7092 7098.
43. Medium Chain Acyl-CoA Dehydrogenase: Aspects of the Reductive Half Reaction; Thorpe, C. (1987) in Flavins and Flavoproteins (Edmondson, D. E., and McCormick, D. B., eds.) Walter de Gruyter, New York, pp. 149 157.
44. Reaction of Medium Chain Acyl-CoA Dehydrogenase with -Oxidation Intermediates; Powell, P. J., Lau, S-M., and Thorpe, C. (1987) in Flavins and Flavoproteins (Edmondson, D. E., and McCormick, D. B., eds.) Walter de Gruyter, New York, pp. 169-172.
45. Medium Chain Acyl-CoA Dehydrogenase: Inactivation of the Reduced Enzyme with 2-Octynol-CoA; Zhou, J-Z., and Thorpe, C. (1987) in Flavins and Flavoproteins (Edmondson, D. E., and McCormick, D. B., eds.) Walter de Gruyter, New York, pp. 173-176.
46. Oxidation and Reduction of Acyl-CoA Dehydrogenase by the Butyryl-CoA/crotonyl-CoA Couple. A New Investigation by Rapid Reaction Kinetics (1987) in Flavins and Flavoproteins (Edmondson, D. E., and McCormick, D. B., eds.) Walter de Gruyter, New York, pp. 177-180.
47. The Interaction of Acyl-CoA Substrates and Analogs with Pig Kidney Medium Chain Acyl-CoA Dehydrogenase; Powell, P. J., Lau, S-M., Killian, D., and Thorpe, C. (1987) Biochemistry 26, 3704-3710.
48. The Nature of Enzyme-Substrate Complexes in the Acyl-CoA Dehydrogenases; Lau, S-M., and Thorpe, C. (1988) Arch. Biochem. Biophys. 262, 293-297.
49. The Reductive Half-Reaction in Acyl-CoA Dehydrogenase from Pig Kidney: Studies with Thia-octanoyl-CoA and Oxa-octanoyl-CoA Analogs; Lau, S-M., Brantley, R. K., and Thorpe, C. (1988) Biochemistry 27, 5089-5095.
50. Oxidation-Reduction of General Acyl-CoA Dehydrogenase by the Butyryl-CoA/Crotonyl-CoA Couple; Schopfer, L. M., Massey, V., Ghisla, S., and Thorpe, C. (1988) Biochemistry 27, 6599-6611.
51. 2-Octynoyl-CoA Is a Mechanism-Based Inhibitor of Pig Kidney Medium Chain Acyl-CoA Dehydrogenase: Isolation of the Target Peptide; Powell, P. J., and Thorpe, C. (1988) Biochemistry 27, 8022-8028.
52. Inactivation of Two Electron Reduced Medium Chain Acyl-CoA Dehydrogenases in Fatty Acid Oxidation; Zhou, J-Z., and Thorpe, C. (1989) Arch. Biochem. Biophys. 271, 261-269.
53. Green Enzymes and Suicide Substrates: A Look at the Acyl-CoA Dehydrogenases in Fatty Acid Oxidation; Thorpe, C. (1989) TIBS, 148-151.
54. 4-Thia-trans-2-alkenoyl-CoA Derivatives: Properties and Enzymatic Reactions; Lau, S-M., Brantley, R. K., and Thorpe, C. (1989) Biochemistry 28, 8255-8262.
55. The Reductive Half Reaction in the Acyl-CoA Dehydrogenases; Thorpe, C. (1989) in Fatty Acid Oxidation: Clinical, Biochemical and Molecular Aspects (Tanaka, K., and Coates, P. M., eds.) Alan R. Liss, New York, pp. 91-106.
56. The L-Hydroxyacyl-CoA Deficiency; Hale, D. E., Thorpe, C., Braat, K., Wright, J. H., Roe, C. R., Coates, P. M., Hashimoto, T., and Glasgow, A. M. (1989) in Fatty Acid Oxidation: Clinical, Biochemical and Molecular Aspects (Tanaka, K., and Coates, P. M., eds.) Alan R. Liss, New York, pp. 503-510.
57. An Acyl-CoA Dehydrogenase Assay Utilizing the Ferricenium Ion; Lehman, T. C., Hale, D. E., Bhala, A., and Thorpe, C. (1990) Anal. Biochem. 186, 280-284.
58. Alternate Electron Acceptors for Medium-Chain Acyl-CoA Dehydrogenase: Use of Ferricenium Salts; Lehman, T. C., and Thorpe, C. (1990) Biochemistry 29, 10594-10602.
59. Modulation of Flavin Reactivity in the Acyl-CoA Dehydrogenases; Thorpe, C. (1990) in Flavins and Flavoproteins (Curti, B., Ronchi, S., and Zanetti, G., eds.) Walter de Gruyter, New York, pp. 294-306.
60. Acetolactate Synthase: A Deviant Flavoprotein; Schloss, J. V., Ciskanik, L., Pai, E. F., and Thorpe, C. (1990) in Flavins and Flavoproteins (Curti, B., Ronchi, S., and Zanetti, G., eds.) Walter de Gruyter, New York, pp. 907-914.
61. The Reductive Half-Reaction in Acyl-CoA Oxidase from Candida tropicalis: Interaction with Acyl-CoA Analogues and an Unusual Thioesterase Activity; Wang, R., and Thorpe, C. (1991) Arch. Biochem. Biophys. 286, 504-510.
62. Reactivity of Medium-Chain Acyl-CoA Dehydrogenase Towards Molecular Oxygen; Wang, R., and Thorpe, C. (1991) Biochemistry 30, 7895-7901.
63. Electron Transferring Flavoproteins; Thorpe C. (1991) in The Chemistry and Biochemistry of Flavoenzymes II (Muller, F., ed.) CRC Press, Boca Raton, Fla., 471-486.
64. A New Form of Mammalian Electron-Transferring Flavoprotein; Lehman, T.C., and Thorpe, C. (1992) Arch. Biochem. Biophys. 292, 594-599.
65. Reductive Half-Reaction in Medium Chain Acyl-CoA Dehydrogenase: Modulation of Internal Equilibrium by Carboxylation of a Specific Methionine Residue; Cummings, J.C., Lau, S-M., Powell, P.J., and Thorpe, C. (1992) Biochemistry, 31, 8523-8529.
66. Stereoselective Interaction of 2-Halo-Acyl-CoA Derivatives with Medium Chain Acyl-CoA Dehydrogenase. Cummings, J.C. and Thorpe, C. (1993) Arch. Biochem. Biophys. 302, 85-91.
67. Inactivation of Short Chain Acyl-CoA Dehydrogenase from Pig Liver by 2-Pentynoyl-CoA. Lundberg, N.N. and Thorpe, C. (1993) Arch. Biochem. Biophys. 306, 454-459.
68. Two New Mechanism-based Inhibitors of the Acyl-CoA Dehydrogenases. Cummings, J.G. and Thorpe, C. (1994) in Flavins and Flavoproteins (Yagi, K. Ed.) pp. 313-321, de Gruyter, Berlin.
69. 3-Methyleneoctanoyl-CoA and 3-Methyl-trans-2-octenoyl-CoA: Two New Mechanism-Based Inhibitors of Medium Chain Acyl-CoA Dehydrogenase from Pig Kidney. Cummings, J.G. and Thorpe, C. (1994) Biochemistry 33, 788-797.
70. Electron-transferring Flavoprotein from Pig and the Methylotrophic Bacterium W3A1 Contains AMP as well as FAD. DuPlessis, E.R., Rohlfs, R.J., Hille, R. and Thorpe, C. (1994) Biochemistry and Molecular Biology International 32, 195-199.
71. S-2-Bromo-acyl-CoA Analogues are Affinity Labels for the Medium Chain Acyl-CoA Dehydrogenase from Pig Kidney. Haeffner-Gormley, L., Cummings, J.G., & Thorpe, C. (1995) Arch. Biochem. Biophys. 217, 479-486.
72. Medium-Chain Acyl-CoA Dehydrogenase- and Enoyl-CoA Hydratase-Dependent Bioactivation of 5,6-Dichloro-4-thia-5-hexenoyl-CoA. Fitzsimmons, M.J., Thorpe, C., and Anders, M.W. (1995) Biochemistry 34, 4276-4286.
73. Structure and Mechanism of Action of the Acyl-CoA Dehydrogenases. Thorpe, C., & Kim, J.J.P. (1995) FASEB Journal 9, 718-725.
74. The Role of the Carbonyl Group in Thioester Chain Length Recognition by the Medium Chain Acyl-CoA Dehydrogenase. Trievel, R.C., Wang, R., Anderson, V.E., & Thorpe, C. (1995) Biochemistry 34, 8457-8605.
75. Fourier-Transform Ion Cyclotron Resonance Mass Spectrometric Evidence for the Formation of -Chloroethenethiolates and Thioketenes from Chloroalkene-Derived Cytotoxic 4-Thia-alkanoates. Zhang, T-l., Wang, L., Hashmi, M., Anders, M.W., Thorpe, C., and Ridge, D.P. (1995) Chemical Research in Toxicology 8, 907-910.
76. Oxidative Inactivation of a Charge Transfer Complex in the Medium Chain Acyl-CoA Dehydrogenase. Schaller, R.A. and Thorpe, C. (1995) Biochemistry 34, 16424-16432.
77. A Sulfhydryl Oxidase from Chicken Egg White. Hoober, K.L., Joneja, B., White, H.B. III, and Thorpe, C. (1996) J. Biological Chemistry 271, 30510-30516.
78. The Acyl-CoA Dehydrogenases: Some Mechanistic Aspects. Thorpe, C., Schaller, R.A., Mohsen, A-W.A. and Vockley, J. (1997) Flavins and Flavoproteins (Stevenson, K.J., Massey, V., and Williams, C.H., eds.) University of Calgary Press, pp. 597-604.
79. Sulfhydryl Oxidase from Egg White. Hoober, K.L., Joneja, B., White, H.B. III, and Thorpe, C. (1997) Flavin and Flavoproteins (Stevenson, K.J., Massey, V., and Williams, C.H., eds.) University of Calgary Press, pp. 807-809.
80. Mechanism-based Inhibitor Discrimination in the Acyl-CoA Dehydrogenases. Schaller, R., Mohsen, A-W. A., Vockley, J., and Thorpe, C. (1997) Biochemistry 36, 7761-7768.
81. Elimination Reactions in the Medium Chain Acyl-CoA Dehydrogenase: Bioactivation of Cytotoxic 4-Thiaalkanoic Acids. Baker-Malcolm, J.F., Haeffner-Gormley, Wang, L., Anders, M.W. and Thorpe, C. (1998) Biochemistry 37, 1383-1393.
82. Protonic Equilibria in the Reductive Half-Reaction of the Medium Chain Acyl-CoA Dehydrogenase. Rudik, I., Ghisla, S., and Thorpe, C. (1998) Biochemistry 37, 8437-8445.
83. The Oxidase Activity of the Acyl-CoA Dehydrogenases. DuPlessis, E.R., Pellet, J., Stankovich, M.T., and Thorpe, C. (1998) Biochemistry 37, 10469-10477.
84. Egg White Sulfhydryl Oxidase: Kinetic Mechanism of the Catalysis of Disulfide Bond Formation. Hoober, K.L., and Thorpe, C. (1999) Biochemistry 38, 3211-3217.
85. Sulfhydryl Oxidase from Egg White: A Facile Catalyst for Disulfide Bond Formation in Proteins and Peptides. Hoober, K.L., Sheasley, S.L., Gilbert, H.F., and Thorpe, C. (1999) J. Biol. Chem (1999) 274, 22147-22150.
86. Homology between egg White Sulfhydryl Oxidase and Quiescin Q6 Defines a New Class of Flavin-linked Sulfhydryl Oxidases. Hoober, K.L., Glynn, N.M., Coppock, D.L. and Thorpe, C. (1999) J. Biol Chem. 274, 31759-31762.
87. 4-Hydroxycinnamoyl-CoA: An Ionizable Probe of the Active Site of the Medium-chain Acyl-CoA Dehydrogenase. Rudik, I., Bell, A., Tonge, P.J. and Thorpe, C. (2000) Biochemistry 39, 92-101.
88. Bioactivation of 5,6-Dichloro-4-thia-5-hexenoyl-CoA by the Medium-chain Dehydrogenase: Mechanism-based Inactivation by a Cytotoxic Thioester. Baker-Malcolm, J.F., Anders, M.W., Wang, M., Kim, J.-J.P., and Thorpe, C. (2000) Flavins and Flavoproteins (Ghisla, S., eds) pp. 499-502.
89. Probing the Active site of the Medium-chain Acyl-CoA Dehydrogenase: 4-OH-cinnamoyl-CoA as a Sensitive Probe of Polarization and Ionization. Rudik, I., Thorpe, C., Bell., A. and Tonge, P.J. (2000) Flavins and Flavoproteins (Ghisla, S., eds) pp. 527-530.
90. Egg White Sulfhydryl Oxidase: Convergent Evolution and Catalysis of Disulfide Bond Formation in Proteins and Peptides. Hoober, K.L., Coppock, D.L., and Thorpe, C. (2000) Flavins and Flavoproteins (Ghisla, S., eds) pp. 685-690.
91. 2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid beta-oxidation. Liang X, Thorpe C, Schulz H. (2000) Arch Biochem Biophys 380, 373-379.
92. Novel Inactivation of Enoyl-CoA Hydratase via -Elimination of 5,6-Dichloro-7,7,7-trifluoro-4-thia-5-heptenoyl-CoA. Baker-Malcolm, J.F., Lantz, M., Anderson, V.E., and Thorpe, C. (2000) Biochemistry, Biochemistry 39, 12007-18
93. Thioester Enolate Stabilization in the Acyl-CoA Dehydrogenases: The Effect of 5-Deaza-flavin Substitution. Rudik, I., and Thorpe, C. (2001) Archives of Biochemistry and Biophysics 392, 341-348.
94. Interaction of 3,4-dienoyl-CoA thioesters with medium chain acyl-CoA dehydrogenase: stereochemistry of inactivation of a flavoenzyme. Wang W, Fu Z, Zhou JZ, Kim JJ, Thorpe C . (2001) Biochemistry 40, 12266-12275.
95. Flavin-Dependent Sulfhydryl Oxidases in Protein Disulfide Bond Formation. Hoober, K.L. and Thorpe, C. (2002) Methods in Enzymology Volume 348 pp. 30-34.
96. C-H…Carboxylate Oxygen Hydrogen Bonding in Substrate Activation by Acyl-CoA Dehydrogenases: Synergy between the H-bonds. Bach, RD., Thorpe, C. and Dimtrenko, O. (2002) J. Phys. Chem. 106: (16) 4325-4335.
97. A Continuous Fluorescence Assay for Sulfhydryl Oxidase. Raje, S., Glynn, N.M. and Thorpe, C. (2002) Analytical Biochemistry 307, 266-272.
98. Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Thorpe, C., Hoober, K.L., Raje, S., Glynn, N.M., Burnside, J., Turi, G.K., and Coppock, D.L. (2002) Arch. Biochem. Biophys. 405, 1-12
99. Effects of As(III) Binding on Alpha-helical Structure. Cline, D., Thorpe, C., and Schneider, J.P. (2003) J. Amer. Chem. Soc. 125, 2923-2529.
100. Inter-Domain Redox Communication in Flavoenzymes of the Quiescin/Sulfhydryl Oxidase Family: Role of a Thioredoxin Domain in Disulfide Bond Formation. Raje, S. and Thorpe, C. (2003) Biochemistry 42, 4560 – 4568
101. Avian Sulfhydryl Oxidase is not a Metalloenzyme: Adventitious Binding of Divalent Metal Ions to the Enzyme. Brohawn, S.G., Rudik, I.R. and Thorpe, C. (2003) Biochemistry 42, 11074-82.
102. Acyl-CoA Dehydrogenases: a Mechanistic Overview. Ghisla, S. and Thorpe, C. (2004) Eur. J. Biochem. 271, 494-508.
103. Effect of the charge-transfer Interaction on the Catalytic Activity of Acyl-CoA Dehydrogenase. Bach, R.D., Thorpe, C. and Dmitrenko, O. (2003) J. Phys. Chem. B 107, 13229-13236.
104. Structure Based design of a Fluorimetric Redox-active Peptide Probe. Cline, D.J., Thorpe, C., and Schneider, J.P. (2004) Anal. Biochem. 325, 144-150.
105. New Water-soluble Phosphines as Reductants of Peptide and Protein Disulfide Bonds: Reactivity and Membrane Permeability. Cline, D.J., Redding, S.E., Brohawn, S.G., Psathas, J.N., Schneider, J.P., and Thorpe, C. (2004) Biochemistry, 43, 15195-15203.
106. General method for facile intramolecular disulfide formation in synthetic peptides. Cline, D.J., Thorpe, C. and Schneider, J.P (2004) Analytical Biochemistry, 335, 168-170.
107. Acyl-CoA dehydrogenases. A mechanistic overview. Ghisla, S. and Thorpe, C. (2004) Eur J Biochem. 2004 Feb;271(3):494-508.
108. Augmenter of Liver Regeneration: a Flavin-dependent Sulfhydryl Oxidase with Cytochrome c Reductase Activity. Farrell, S.R. and Thorpe, C. (2005) Biochemistry 44, 1532-41.
109. Multi-domain Flavin-dependent Sulfhydryl Oxidases. Coppock, D.L. and Thorpe, C. (2006) Antioxidants and Redox Signalling, 8, 300-311.
110. Flavin-dependent Sulfhydryl Oxidases. Thorpe, C. (2005) Flavins and Flavoproteins, (T. Nishino, R. Miura, M. Tanokura, and K. Fukui Eds.) pp. 331-339, ARchiTect Inc.
111. Generating Disulfides Enzymatically: Reaction Products and Electron Acceptors of the Endoplasmic Reticulum Thiol Oxidase Ero1p. Gross, E., Sevier, C.S., Heldman, N., Vitu, E., Bentzur, M., Kaiser, C.A., Thorpe, C., and Fass, D. (2006) Proc. Nat. Acad. Sci. 103, 299-304.
112. Determination of the Distance between the Two Neutral Flavin Radicals in Augmenter of Liver Regeneration by Pulsed ELDOR. Kay, K.W.M., Elsasser, C., Bittl, R., Farrell, S.R., and Thorpe, C. (2006) J. Am. Chem. Soc. 128(1):76-7.
113. Erv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase. Wang, W., Winther, J.R. , and Thorpe, C. (2007) Biochemistry, 46(11) 3246-54.
114. Effects of As(III) Binding on beta-Hairpin Structure. Ramadan, D., Cline, D.J., Thorpe, C. and Schneider, J.P. (2007) J. Amer. Chem. Soc. 129(10), 2981-2988 .
115. Generating disulfides in multicellular organisms: emerging roles for a new flavoprotein family. Thorpe, C and Coppock, D.L. (2007) J. Biol. Chem. 282, 13929-13933.
115. The Mechanism of SN2 Disulfide Bond Cleavage by Phosphorous Nucleophiles. Implications for Biochemical Disulfide Reducing Agents. (2007) Dmitrenko, O., Thorpe, C. and Bach, R. J. Org. Chem. 72, 8298-8307.
116 The Mechanism of Thiolate-disulfide Interchange Reactions in Biochemistry. Bach, R., Dmitrenko, O., and Thorpe, C. (2008) J. Org. Chem. 73, 12-21.
117 Generating disulfides with the quiescin sulfhydryl oxidases. Heckler, E.J., Rancy, P.C., Kodali, V.K., Thorpe, C. (2008) Biochim. Biophys. Acta. – Molecular Cell Research, 1783(4):567-77.
118 A Flavin-dependent Sulfhydryl Oxidase in Bovine Milk. Jaje, J., Wolcott, H.N., Fadugba, O., Cripps, D., Yang, A.J., Mather, I.H., and Thorpe, C. (2007) Biochemistry, 46, 13031-40.
119. Human Quiescin sulfhydryl oxidase, QSOX1: Probing Internal Redox Steps by Mutagenesis (2008) Heckler, E.J., Alon, A., Fass, D., and Thorpe, C. (2008) Biochemistry. 29;47(17):4955-63.
120. A Computational Analysis of the Interaction between Flavin and Thiol(ate) Groups. Implications for Flavoenzyme Catalysis. Dmitrenko, O., and Thorpe, C. (2008) J. Sulfur Chemistry, 29, 415-424
121. Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase. Rancy P.C. and Thorpe C. (2008) Biochemistry. 18;47(46):12047-56.
122. Arsenic(III) Species Inhibit Oxidative Protein Folding in vitro. Ramadan, D., Rancy, P.C., Nagarkar, R.P., Schneider, J.P., and Thorpe, C. (2009) Biochemistry 20, 424-432.
123. Augmenter of Liver Regeneration: Substrate Specificity of a Flavin-dependent Oxidoreductase from the Mitochondrial Intermembrane Space. Daithankar, V.K. Farrell, S.R., and Thorpe, C. (2009) Biochemistry, 48(22):4828-37.
124. Quiescin Sulfhydryl Oxidase from Trypanosoma brucei: Catalytic Activity and Mechanism of a QSOX Family Member with a Single Thioredoxin Domain. Kodali, V.K. and Thorpe, C. (2010) Biochemistry 49, 2075-85 [PubMed]
125. Oxidative Protein Folding and the Quiescin-sulfhydryl Oxidase Family of Flavoproteins. Kodali VK., Thorpe, C. (2010) Antioxid Redox Signal. 13, 1217-30. [PubMed]
126. QSOX Contains a Pseudo-dimer of Functional and Degenerate Sulfhydryl Oxidase Domains. Alon, A., Heckler, E.J., Thorpe, C. and Fass, D. (2010) FEBS letters, 584, 1521-1525. [PubMed]
127. A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity. Blais JD, Chin KT, Zito E, Zhang Y, Heldman N, Harding HP, Fass D, Thorpe C, Ron D. (2010) J. Biol. Chem. 285, 20993-21003 [PubMed]
128. Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy. Daithankar, V.N., Schaefer, S.A., Dong, M., Bahnson, B.J., and Thorpe, C. (2010) Biochemistry 49, 6737-45 [PubMed]
129. A Novel Disulfide-Rich Protein Motif from Avian Eggshell Membranes. Kodali, V.K., Gannon, S.A., Paramasivam, S., Raje, S., Polenova, T., and Thorpe, C. (2011) PLoS ONE 6, 1-11. [PubMed]
130. Flavin-linked Erv-family sulfhydryl oxidases release superoxide anion during catalytic turnover. Daithankar, V.N., Wang, W., Trujillo, J., and Thorpe, C. (2012) Biochemistry, 51, 265-272. [PubMed]
131. Protein Substrate Discrimination in the Quiescin Sulfhydryl Oxidase (QSOX) Family. Codding, J.A., Israel, B.A., and Thorpe, C. (2012) Biochemistry 22, 4226-35. [PubMed]
132. The dynamic disulphide relay of quiescin sulphydryl oxidase. Alon A, Grossman I, Gat Y, Kodali VK, Dimaio F, Mehlman T, Haran G, Baker D, Thorpe C, Fass D. (2012) Nature. Aug 16;488(7411):414-8. [PubMed]
133. 77Se Enrichment of Proteins Expands the Biological NMR Toolbox. Schaefer SA, Dong M, Rubenstein RP, Wilkie WA, Bahnson BJ, Thorpe C, Rozovsky S. (2012) J Mol Biol., 425, 221-231. [PubMed]
134. Flavoproteins in Oxidative Protein Folding. Thorpe C. (2012) in Handbook of Flavoproteins, Volume 1: Oxidases, Dehydrogenases and Related Systems (Hille, R., Miller, S. and Pafey, B. eds.) pp. 249-270.
135. An Arsenical-maleimide for the Generation of New Targeted Biochemical Reagents. Sapra, A., and Thorpe, C. (2013) J. Am. Chem. Soc. Publication Date (Web): February 5, 2013 (Communication). [PubMed]
136. Quantification of Thiols and Disulfides. Winther, J.R. and Thorpe, C. (2014) Biochim. Biophys. Acta 1840, 838-846. [PubMed]
137. Human Augmenter of Liver Regeneration; probing the catalytic mechanism of a flavin-dependent sulfhydryl oxidase. Schaefer-Ramadan, S., Gannon, S.A., and Thorpe, C. (2013) Biochemistry, 52, 8323-8332. [PubMed]
138. Going Through the Barrier: Coupled Disulfide Exchange Reactions Promote Efficient Catalysis in Quiescin Sulfhydryl Oxidase. (2013) Israel, B.A., Kodali, V.K., and Thorpe, C. J. Biol. Chem., 289, 5274-5284. [PubMed]
139. Disulfide bond generation in mammalian blood serum; detection and purification of Quiescin-sulfhydryl oxidase (2014) Israel, B.A., Jiang, L., Gannon, S.A., and Thorpe, C. Free Radical Biology and Medicine, 69, 129-135. [PubMed]
140. Site-specific insertion of selenium into the redox-active disulfide of the flavoprotein Augmenter of Liver Regeneration. Schaefer-Ramadan, S., Thorpe, C., and Rozovsky, S. (2014) Archives of Biochemistry and Biophysics, 548, 60-65. [PubMed]
141. Oxidative Protein Folding: from Thiol-disulfide Exchange Reactions to the Redox Poise of the Endoplasmic Reticulum. Hudson, D.A., Gannon, S.A. and Thorpe, C. (2014) Free Radical Biology and Medicine [PubMed].
142. Multivalency in the Inhibition of Oxidative Protein Folding by Arsenic (III) Species. Sapra, A., Ramadan, D. and Thorpe, C. (2014) Biochemistry, in press [PubMed]
143. Mia40 is a facile oxidant of unfolded reduced proteins but shows minimal isomerase activity. Hudson, D.A. and Thorpe, C. (2015) Archives of Biochemistry and Biophysics, 579, 1-7. [PubMed]
144. Rapid Bioorthogonal Chemistry Turn-on through Enzymatic or Long Wavelength Photocatalytic Activation of Tetrazine Ligation. Zhang H, Trout WS, Liu S, Andrade GA, Hudson DA, Scinto SL, Dicker KT, Li Y, Lazouski N, Rosenthal J, Thorpe C, Jia X, Fox JM. (2016) J Am Chem Soc. 138, 5978-83 [PubMed]
145. Challenges in the Evaluation of Thiol-reactive Inhibitors of Human Protein Disulfide Isomerase. Foster, C.K. and Thorpe, C. (2017) Free Radic. Biol. Med. 108, 741-749. [PubMed]
146. Chemistry and Enzymology of Disulfide Cross-linking in Proteins. Fass, D. and Thorpe, C. (2017) Chemical Reviews 118, 1169-1198. [PubMed]
147. Designing Flavoprotein-GFP Fusion Probes for Analyte_Specific Ratiometric Fluorescence Imaging. Hudson, D.A. Caplan, J.L. Thorpe,C. (2018) Biochemistry 57, 1178-1189. [PubMed]
148. Gaussia princeps luciferase: a bioluminescent substrate for oxidative protein folding. Yu, T. Laird, J.R., Prescher, J.A. and Thorpe, C. (2018) Protein Science (in press) [PubMed]