ROBERT J contact HONDAL

Summary

Affiliation: University of Vermont
Country: USA

Publications

  1. pmc Selenocysteine in thiol/disulfide-like exchange reactions
    Robert J Hondal
    Given Laboratory, Department of Biochemistry, University of Vermont, Burlington, VT 05405, USA
    Antioxid Redox Signal 18:1675-89. 2013
  2. pmc Incorporation of selenocysteine into proteins using peptide ligation
    Robert J Hondal
    Department of Biochemistry, Vermont College of Medicine, The University of Vermont, Burlington, VT 05405, USA
    Protein Pept Lett 12:757-64. 2005
  3. pmc Differing views of the role of selenium in thioredoxin reductase
    Robert J Hondal
    Department of Biochemistry, College of Medicine, University of Vermont, Burlington, 05405, USA
    Amino Acids 41:73-89. 2011
  4. pmc Using chemical approaches to study selenoproteins-focus on thioredoxin reductases
    Robert J Hondal
    Department of Biochemistry, University of Vermont, College of Medicine, 89 Beaumont Ave, Given Building Room B413, Burlington, VT 05405, USA
    Biochim Biophys Acta 1790:1501-12. 2009
  5. pmc No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue
    Adam P Lothrop
    Department of Biochemistry, University of Vermont, 89 Beaumont Avenue, Given Building Room B413, Burlington, Vermont 05405, USA
    Biochemistry 48:6213-23. 2009
  6. pmc Synthesis of peptide substrates for mammalian thioredoxin reductase
    Stevenson Flemer
    Department of Biochemistry, Given Laboratory, Burlington, VT 05405, USA
    J Pept Sci 14:637-47. 2008
  7. ncbi request reprint Semisynthesis of proteins containing selenocysteine
    Robert J Hondal
    Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA
    Methods Enzymol 347:70-83. 2002
  8. pmc Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases
    Brian E Eckenroth
    Department of Biochemistry, University of Vermont College of Medicine, 89 Beaumont Avenue, Burlington, Vermont 05405, USA
    Biochemistry 46:4694-705. 2007
  9. pmc Semisynthesis and characterization of mammalian thioredoxin reductase
    Brian Eckenroth
    Department of Biochemistry, University of Vermont, 89 Beaumont Avenue, Given Laboratory, Room B413, Burlington, Vermont 05405, USA
    Biochemistry 45:5158-70. 2006
  10. pmc Selenium in thioredoxin reductase: a mechanistic perspective
    Brian M Lacey
    Department of Biochemistry, College of Medicine, University of Vermont, 89 Beaumont Avenue, Given Building Room B413, Burlington, Vermont 05405, USA
    Biochemistry 47:12810-21. 2008

Research Grants

Collaborators

Detail Information

Publications13

  1. pmc Selenocysteine in thiol/disulfide-like exchange reactions
    Robert J Hondal
    Given Laboratory, Department of Biochemistry, University of Vermont, Burlington, VT 05405, USA
    Antioxid Redox Signal 18:1675-89. 2013
    ..Sec differs from cysteine (Cys) by only one atom (selenium versus sulfur), yet this switch dramatically influences important aspects of enzyme reactivity...
  2. pmc Incorporation of selenocysteine into proteins using peptide ligation
    Robert J Hondal
    Department of Biochemistry, Vermont College of Medicine, The University of Vermont, Burlington, VT 05405, USA
    Protein Pept Lett 12:757-64. 2005
    ..This replacement can confer unique structural and catalytic properties to enzymes and proteins. The development of this technique also allows for naturally occurring selenoproteins to be produced semisynthetically...
  3. pmc Differing views of the role of selenium in thioredoxin reductase
    Robert J Hondal
    Department of Biochemistry, College of Medicine, University of Vermont, Burlington, 05405, USA
    Amino Acids 41:73-89. 2011
    ....
  4. pmc Using chemical approaches to study selenoproteins-focus on thioredoxin reductases
    Robert J Hondal
    Department of Biochemistry, University of Vermont, College of Medicine, 89 Beaumont Ave, Given Building Room B413, Burlington, VT 05405, USA
    Biochim Biophys Acta 1790:1501-12. 2009
    ..The enzyme utilizes a macromolecular mechanism for protein substrates, a second mechanism for small molecule substrates and a third pathway for selenium-containing substrates such as selenocystine...
  5. pmc No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue
    Adam P Lothrop
    Department of Biochemistry, University of Vermont, 89 Beaumont Avenue, Given Building Room B413, Burlington, Vermont 05405, USA
    Biochemistry 48:6213-23. 2009
    ..7 in the full-length mammalian enzyme (83-142 nM), but surprisingly the truncated enzyme showed much stronger inhibition (25 nM). This contrasts with auranofin, where the absence of Sec more strongly perturbed inhibition...
  6. pmc Synthesis of peptide substrates for mammalian thioredoxin reductase
    Stevenson Flemer
    Department of Biochemistry, Given Laboratory, Burlington, VT 05405, USA
    J Pept Sci 14:637-47. 2008
    ..The results show that the ring structure contributes a factor of 52 to the rate, but the presence of selenium in the peptide is more important to catalysis than the presence of the ring...
  7. ncbi request reprint Semisynthesis of proteins containing selenocysteine
    Robert J Hondal
    Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA
    Methods Enzymol 347:70-83. 2002
  8. pmc Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases
    Brian E Eckenroth
    Department of Biochemistry, University of Vermont College of Medicine, 89 Beaumont Avenue, Burlington, Vermont 05405, USA
    Biochemistry 46:4694-705. 2007
    ..This places the Sec residue farther away from the protonating histidine residue, but the lower pKa of Sec in comparison to that of Cys eliminates the need for Sec to be protonated...
  9. pmc Semisynthesis and characterization of mammalian thioredoxin reductase
    Brian Eckenroth
    Department of Biochemistry, University of Vermont, 89 Beaumont Avenue, Given Laboratory, Room B413, Burlington, Vermont 05405, USA
    Biochemistry 45:5158-70. 2006
    ..This noncovalent peptide-enzyme complex has 350-500-fold lower activity than the semisynthetic enzyme produced by peptide ligation...
  10. pmc Selenium in thioredoxin reductase: a mechanistic perspective
    Brian M Lacey
    Department of Biochemistry, College of Medicine, University of Vermont, 89 Beaumont Avenue, Given Building Room B413, Burlington, Vermont 05405, USA
    Biochemistry 47:12810-21. 2008
    ..Further study of the biochemical properties of the truncated Cys and Sec TR enzymes demonstrates that the chemical advantage conferred on the eukaryotic enzyme by a selenol is the ability to function at acidic pH...
  11. pmc Studies on deprotection of cysteine and selenocysteine side-chain protecting groups
    Katharine M Harris
    Department of Biochemistry, 89 Beaumont Ave, Given Laboratory, Room B413, Burlington, VT 05405, USA
    J Pept Sci 13:81-93. 2007
    ....
  12. pmc Characterization of mitochondrial thioredoxin reductase from C. elegans
    Brian M Lacey
    Department of Biochemistry, 89 Beaumont Ave, Given Laboratory, Room B413, Burlington, VT 05405, USA
    Biochem Biophys Res Commun 346:629-36. 2006
    ..The enzyme would reduce selenocysteine, but not hydrogen peroxide or insulin. The flanking glycine residues of the GCCG motif were mutated to serine. The mutants improved substrate binding, but decreased the catalytic rate...

Research Grants7

  1. Selenium-Thioredoxin Reductase Studied by Semisynthesis
    ROBERT HONDAL; Fiscal Year: 2009
    ..The importance of the thioredoxin system in disease processes such as cancer, arthritis, and malaria gives impetus to the study of the enzyme mechanism for the development of potential therapeutic inhibitors. ..
  2. The Biological and Chemical Function of Selenium in Enzymes
    ROBERT J contact HONDAL; Fiscal Year: 2010
    ..Cancer cells must divide rapidly to cause pathogenesis and require increased expression of thioredoxin reductase to survive. ..