Publications

QSOX Articles

complete publication list is here

  • 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]
  • 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]
  • 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. 2012 Aug 16;488(7411):414-8. [PubMed]
  • 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]
  • 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]
  • 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]
  • 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 47, 12047-56. [PubMed]
  • Human Quiescin sulfhydryl oxidase, QSOX1: Probing Internal Redox Steps by Mutagenesis (2008) Heckler, E.J., Alon, A., Fass, D., and Thorpe, C. (2008) Biochemistry 47, 4955-63. [PubMed]
  • 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. [PubMed]
  • 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. [PubMed]
  • 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 [PubMed]
  • 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. [PubMed]
  • 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. 274, 22147-22150. [PubMed]
  • Egg White Sulfhydryl Oxidase:  Kinetic Mechanism of the Catalysis of Disulfide Bond Formation.  Hoober, K.L., and Thorpe, C. (1999) Biochemistry 38, 3211-3217. [PubMed]
  • A Sulfhydryl Oxidase from Chicken Egg White.  Hoober, K.L., Joneja, B., White, H.B. III, and Thorpe, C. (1996) J. Biol. Chem. 271, 30510-30516. [PubMed]

Review Articles

complete publication list is here

  • Chemistry and Enzymology of Disulfide Cross-linking in Proteins. Fass, D. and Thorpe, C. (2017) Chemical Reviews 118, 1169-1198. [PubMed]
  • 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, 80, 171-182.
  • Quantification of Thiols and Disulfides.  Winther, J.R. and Thorpe, C. (2013) Biochim. Biophys. Acta, 1840, 838-846 [PubMed]
  • 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.
  • Oxidative Protein Folding and the Quiescin-sulfhydryl Oxidase Family of Flavoproteins.  Kodali VK., Thorpe, C. (2010) Antioxid Redox Signal. Feb 6. [Epub ahead of print] [PubMed]
  • 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, 567-77. [PubMed]
  • 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. [PubMed]
  • Multi-domain Flavin-dependent Sulfhydryl Oxidases.  Coppock, D.L. and Thorpe, C. (2006) Antioxidants and Redox Signaling, 8, 300-311. [PubMed]
  • 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.
  • 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. [PubMed]

Augmenter of Liver Regeneration and Erv2p

complete publication list is here

  • 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, in press.
  • 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]
  • 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]
  • 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]
  • 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]
  • Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy.  (2010) Daithankar, V.N., Schaefer, S.A., Dong, M., Bahnson, B.J., and Thorpe, C. (2010) Biochemistry 49, 6737-6745.  [PubMed]
  • 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, 4828-37. [PubMed]
  • Erv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase.  Wang, W., Winther, J.R. , and Thorpe, C. (2007) Biochemistry, 46, 3246-54. [PubMed]
  • 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, 76-7. [PubMed]
  • 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. [PubMed]

 

Ero1 and Ero1L oxidases

complete publication list is here

  • 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. May 4. [PubMed, Epub ahead of print]
  • 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. [PubMed]

 

Methods and Miscellaneous

complete publication list is here

  • 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]
  • 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]
  • 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]
  • 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. 2016 Apr 27. [Epub ahead of print] [PubMed]
  • 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, 80, 171-182.
  • 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]
  • Quantification of Thiols and Disulfides.  Winther, J.R. and Thorpe, C. (2014) Biochim. Biophys. Acta 1840, 838-846. [PubMed]
  • 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. [Ref]
  • 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. [PubMed]
  • 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. [PubMed]
  • A Continuous Fluorescence Assay for Sulfhydryl Oxidase.  Raje, S., Glynn, N.M. and Thorpe, C. (2002) Anal. Biochem. 307, 266-272. [PubMed]
  • Flavin-Dependent Sulfhydryl Oxidases in Protein Disulfide Bond Formation.  Hoober, K.L. and Thorpe, C. (2002) Methods in Enzymology Volume 348, pp. 30-34. [PubMed]

    Chemical aspects of thiols and disulfides

    complete publication list is here

    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, 80, 171-182.

    Quantification of Thiols and Disulfides.  Winther, J.R. and Thorpe, C. (2013) Biochim. Biophys. Acta, April 6 [PubMed]

    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. [Link]

    The Mechanism of Thiolate-disulfide Interchange Reactions in Biochemistry.  Bach, R., Dmitrenko, O., and Thorpe, C. (2008) J. Org. Chem. 73, 12-21. [PubMed]

    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. [PubMed]

     

    Arsenic effects with peptides, proteins and enzymes

    complete publication list is here

    Multivalency in the Inhibition of Oxidative Protein Folding by Arsenic (III) Species. Sapra, A., Ramadan, D. and Thorpe, C. (2014) Biochemistry, in press [PubMed]

    An Arsenical-maleimide for the Generation of New Targeted Biochemical Reagents.  Sapra, A., and Thorpe, C. (2013) J. Amer. Chem. Soc. Publication Date (Web): February 5, 2013. [PubMed]

    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 48, 424-432. [PubMed]

    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, 2981-2988. [PubMed]

    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. [PubMed]

     

    Publications – Complete List (1970 – Present)