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  People

Nicole Sukdeo
Post-Doctoral Fellow

e-mail: sukdeo_n@gmx.com
office phone: 604-827-4216

Research interests:

  • Nitramine biodegradation specifically hexahydro-1,3,5-trinitro-1,3,5-triazine (also known as "Royal Demolition Explosive, RDX")
  • Microbial community dynamics in RDX contaminated soil

Current Project:
Metagenomic analysis of microbial communities in RDX-contaminated soils

Education:  
2003 - 2008 PhD Department of Chemistry, University of Waterloo, Waterloo, ON
Supervisor: Dr. John F. Honek
Thesis: Enzymology and structure-function studies of bacterial Glyoxalase I enzymes
2000 - 2002 M.Sc. Department of Chemistry, University of Waterloo, Waterloo, ON
Supervisor: Dr. John F. Honek
Comparative biochemistry and mutagenesis studies of bacterial Glyoxalase I enzymes
1996 - 2000 B. Sc. Department of Applied Health Sciences, University of Waterloo, Waterloo, ON
Honours Health Studies, Minor in Chemistry, Minor in Biology

Publications:

Sukdeo, N. & Charles, T.C. Application of crossover-PCR-mediated deletion-insertion mutagenesis to analysis of the bdhA-xdhA2-xdhB2 mixed-function operon of Sinorhizobium meliloti. Archives of Microbiology 179, 301-304 (2003).

Sukdeo, N., Clugston, S.L., Elisabeth, D. & Honek, J.F. Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes. Biochem. J 384, 111-117 (2004).

O'Young, J., Sukdeo, N. & Honek, J.F. Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme. Archives of Biochemistry and Biophysics 459, 20-26 (2007).

Sukdeo, N. & Honek, J.F. Pseudomonas aeruginosa contains multiple glyoxalase I-encoding genes from both metal activation classes. Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 1774, 756-763 (2007).

Sukdeo, N. & Honek, J.F. Microbial glyoxalase enzymes: metalloenzymes controlling cellular levels of methylglyoxal. Drug Metabol Drug Interact 23, 29-50 (2008).

Su, Z., Sukdeo, N. & Honek, J.F. 15N-1H HSQC NMR evidence for distinct specificity of two active sites in Escherichia coli glyoxalase I. Biochemistry 47, 13232-13241 (2008).

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