University of Vermont

College of Medicine

Department of Biochemistry

Bio for Erik Ruggles
Erik Ruggles

Erik Ruggles

Contact Information
Office Location:
Biochemistry, Given B415


Dr. Ruggles received his B.S. in Chemistry from Ithaca College under Heinz Koch where he synthesized highly halogenated styrene analogs. He subsequently got his M.S. in Chemistry from Bucknell University under Thomas T. Shawe where he used a tandem ozonolysis reductive amination approach for the construction of novel quinocarcin analogues. Dr. Ruggles then received his Ph.D. in Organic Chemistry in 2003 from Michigan State University in the lab of Robert E. Maleczka Jr. where he elucidated chlorinative carbocation rearrangements of vinylic carbinols. His postdoctoral training began in the lab of Gregory K. Friestad in the Chemistry Department at the University of Vermont where he studied enantioselective radical additions to N-acylhydrazones mediated by chiral Lewis acids. He then continued his postdoctoral training at UVM in the Biochemistry Department under Robert J. Hondal as a NIH University Postdoctoral Fellow where he investigated the synthesis, conformations, and redox properties of disulfide containing eight-membered rings with application to thioredoxin reductases.

Awards and Honors

2012- 2015    Nominated for Kroepsch-Maurice Award for Teaching Excellence (Lecturer Category)

2008 Excellence in Laboratory Signage and Community Responsibility, University of Vermont

2004-2007 NIH University Postdoctoral Fellow Trainee (PHS T32 HL07594), University of Vermont

2003 Dissertation Completion Fellowship, Michigan State University

1999 Chemistry Travel Award, Michigan State University

1999 Merit Level Teaching Assistantship Award, Michigan State University

1996 Sigma Xi Inductee

1993 NSF Summer Fellowship, Ithaca College and Gorleaus Laboratory


Ruggles, E. L.; Deker, P. B.; Hondal, R. J.  ? Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy?, J. Pept. Sci. 2014, 20, 349-360.

Lothrop, A. P.; Snider, G. W.; Flemer, S. Jr.; Ruggles, E. L.; Davidson, R. S.; Lamb, A.; Hondal, R. J.  ?Compensating for the absence of selenocysteine in high Mr thioredoxin reductases: The electrophilic activation hypothesis?, Biochemistry 2014, 53, 664-674.

Lothrop, A. P.; Snider, G. W.; Ruggles, E. L.; Patel, A. S.; Lees, W. J.; Hondal, R. J.  Selenium as an electron acceptor during the catalytic mechanism of thioredoxin reductase?, Biochemistry 2014, 53, 654-663.

Snider, G. W.; Dustin, C. M.; Ruggles, E. L.; Hondal, R. J.  A mechanistic investigation of the C-terminal redox motif of thioredoxin reductase from Plasmodium falciparum?, Biochemistry 2014, 53, 601-609.

Lothrop, A. P.; Snider, G. W.; Ruggles, E. L.; Hondal, R. J.  Why is mammalian thioredoxin reductase-1 so dependent upon the use of selenium, Biochemistry 2014, 53, 554-565.

Snider, G. W.; Ruggles, E. L.; Khan, N.; Hondal, R. J. Selenocysteine Confers Resistance to Inactivation by Oxidation in Thioredoxin Reductase: Comparison of Selenium and Sulfur Enzymes, Biochemistry 2013, 52, 5472-5481.

Ruggles, E. L.; Snider, G.; Hondal, R. J. Chapter Six, Chemical Basis for the Use of Selenocysteine, In Selenium:  Its Molecular Biology and Role in Human Health; Hatfield, D. L., Berry, M. J., Gladyshev, V. N., Eds.; Springer: New York, 2012, 73-83.

Hondal, R. J.; Ruggles, E. L. Differing views of the role of selenium in thioredoxin reductase Amino Acids 2011, 41, 73-89.

Snider, G.; Grout, L.; Ruggles, E. L.; Hondal, R. J. Methaneseleninic Acid is a Substrate for Truncated Mammalian Thioredoxin Reductase: Implications for the Catalytic Mechanism and Redox Signaling, Biochemistry 2010, 49, 10329-10338.

Lothrop, A. P.; Ruggles, E. L.; Hondal, R. J.  No Selenium Required:  Reactions Catalyzed by Mammalian Thioredoxin Reductase That Are Independent of a Selenocyteine Residue, Biochemistry 2009, 48, 6213-6123.

Ruggles, E. L.; Deker, P. B.; Hondal. R. J.  “Synthesis, Redox Properteis, and Conformational Analysis of Vicinal Disulfide Ring Mimics.” Tetrahedron 2009, 65, 1257-1267