(Feb_08)
___________________________________________________________________________
CURRICULUM VITAE Colin
Thorpe
___________________________________________________________________________
Professor of Biochemistry 98
W. Mill Station Dr.
Department of Chemistry and Biochemistry
Phone: (302)
831-2689 (FAX -6335)
EMail: cthorpe@udel.edu
____________________________________________________________________________
Born: 1947,
in
Marital Status: Married to Minori Thorpe: 2 children
Education:
B.A. (1969)
Ph.D.
(1972)
Postdoctoral
Scholar (1973-1978)
Professional Experience:
1969 -1972: Graduate
student (with Dr. R. D. Gillard, in the Medical Research Council Inorganic
Biochemistry Group,
1973 -1978: Postdoctoral
scholar (with Dr. Charles H. Williams, Jr.,
1978 - : Assistant
Professor (1978-1983); Associate Professor (1983-1989); Full Professor
(1989-present), Department of Chemistry and Biochemistry,
Professional
Organizations:
American
Chemical Society, American Society for Biochemistry and Molecular Biology.
Editorial
Board: Archives of Biochemistry and
Biophysics.
Honors: Co-chair 1990
Enzymes, Coenzymes and Metabolic Pathways Gordon Conference. Organizing committees 12th International
Symposium on Flavins and Flavoproteins,
Service within Department: Recent
committee assignments: Planning Committee, NIH Interface Committee,
Current service within University: Chairman
of University Radiation Safety Committee.
Service outside University: Biochemistry
Study Section Member (2001-2005). Ad hoc
Reviewer for Physical Biochemistry and Biochemistry Study Sections, Reviewer
for Biochemistry, Journal of Biological Chemistry, J. American Chemical Society,
Biochimica et Biophysica Acta, Biochemical Pharmacology, European Journal of
Biochemistry, Chemical Research in Toxicology, Journal of Investigative
Dermatology, Applied and Environmental Microbiology, and for the Australian
Research Board, National Institutes of Health, National Science Foundation,
Veterans Administration Research Service, Petroleum Research Fund and Research
Corporation.
Grants
(current): NIH GM26643-27: "Flavoproteins in Oxidative Protein
Folding" from 1979-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)
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,
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
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
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
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
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
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
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
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
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
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
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,
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,
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
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
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,
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,
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.,
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.)
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.)
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,
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.,
87. 4-Hydroxycinnamoyl-CoA: An Ionizable Probe of the Active Site of the
Medium-chain Acyl-CoA Dehydrogenase. Rudik, I.,
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,
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.,
93. Thioester Enolate Stabilization in the Acyl-CoA
Dehydrogenases: The Effect of
5-Deaza-flavin Substitution. Rudik,
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.,
98. Sulfhydryl oxidases: emerging catalysts of
protein disulfide bond formation in eukaryotes.
Thorpe, C., Hoober, K.L., Raje, S.,
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.
109. 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.
Biochim. Biophys. Acta. –
Molecular Cell Research, 2007 Oct 12 [Epub ahead of print].
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.