Publications

On The Cover:

Left: Säbel, C. E., Neureuther, J. M., Siemann, S. (2010) A spectrophotometric method for the determination of zinc, copper, and cobalt ions in metalloproteins using Zincon. Anal. Biochem. 397, 218-226.

Right: Young, C. J., Siemann, S. (2016) Highly dynamic metal exchange in anthrax lethal factor involves the occupation of an inhibitory metal binding site. Chem. Commun. 52, 11748-11751.

  1. Lo, S.Y., Goulet, D.L., Fraaz, U., Siemann, S. (2020) Effect of pH and denaturants on the fold and metal status of anthrax lethal factor. Arch. Biochem. Biophys. 692, 108547. [pdf]
  2. Goulet, D.L., Fraaz, U., Zulich, C.J., Pilkington, T.J., Siemann, S. (2020) Specificity-directed design of a FRET-quenched heptapeptide for assaying thermolysin-like proteases. Anal. Biochem. 604, 113826. [pdf]
  3. Hume, S., Caron, F., Siemann, S. (2018) Binding of Cu, Co, and Cs to fluorescent components of natural organic matter (NOM) from three contrasting sites. Environ. Sci. Pollut. Res. 25, 20141-20153. [pdf]
  4. Hinchliffe, P., Tanner C. A., Krismanich, A. P., Labbé, G., Goodfellow, V. J., Marrone, L., Desoky, A. Y., Calvopiña, K., Whittle, E. E., Zeng, F., Avison, M. B., Bols, N. C., Siemann, S., Spencer, J., Dmitrienko, G. I. (2018) Structural and kinetic studies on the potent inhibition of metallo-β-lactamases by 6-phosphonomethylpyridine-2-carboxylates. Biochemistry 57, 1880-1892. [pdf]
  5. Young, C. J., Richard, K., Beruar, A., Lo, S. Y., Siemann, S. (2018) An investigation of the pH dependence of copper-substituted anthrax lethal factor and its mechanistic implications. J. Inorg. Biochem. 182, 1-8. [pdf]
  6. Young, C. J., Siemann, S. (2016) Highly dynamic metal exchange in anthrax lethal factor involves the occupation of an inhibitory metal binding site. Chem. Commun. 52, 11748-11751. [pdf] Article featured on the cover of ChemComm.
  7. Riopel, R., Siemann, S., Caron, F. (2016) Microbial changes in the fluorescence character of natural organic matter from a wastewater source. J. Water Resource Prot. 8, 873-883. [pdf] OPEN ACCESS
  8. Rotondo, C. M., Marrone, L., Goodfellow, V. J., Ghavami, A., Labbé, G., Spencer, J., Dmitrienko, G. I., Siemann, S. (2015) Arginine-containing peptides as potent inhibitors of VIM-2 metallo-β-lactamase. Biochim. Biophys. Acta 1850, 2228-2238. [pdf]
  9. Ghavami, A., Labbé, G., Brem, J., Goodfellow, V. J., Marrone, L., Tanner, C. A., King, D. T., Lam, M., Strynadka, N. C. J., Pillai, D. R., Siemann, S., Spencer, J., Schofield, C. J., Dmitrienko, G. I. (2015) Assay for drug discovery: Synthesis and testing of nitrocefin analogues for use as β-lactamase substrates. Anal. Biochem. 486, 75-77. [pdf]
  10. Lo, S. Y., Säbel, C. E., Mapletoft, J. P., Siemann, S. (2015) Influence of chemical denaturants on the activity, fold and metal status of anthrax lethal factor. Biochem. Biophys. Rep. 1, 68-77. [pdf] OPEN ACCESS
  11. Riopel, R., Caron, F., Siemann, S. (2014) Fluorescence Characterization of Natural Organic Matter at a Northern Ontario Waste Water Treatment Plant. Water Air Soil Pollut. 225, 2126. [pdf]
  12. Lo, S. Y., Säbel, C. E., Webb, M. I., Walsby, C. J., Siemann, S. (2014) High metal substitution tolerance of anthrax lethal factor and characterization of its active copper-substituted analogue. J. Inorg. Biochem. 140, 12-22. [pdf]
  13. Xu, L., Ye, Z., Siemann, S., Gu, Z. (2014) Noncovalent Solubilization of Multi-Walled Carbon Nanotubes in Common Low-Polarity Organic Solvents with Branched Pd–Diimine Polyethylenes: Effects of Polymer Chain Topology, Molecular Weight and Terminal Pyrene Group. Polymer 55, 3120-3129. [pdf]
  14. Caron, F., Siemann, S., Riopel, R. (2014) Characterization of the natural organic matter (NOM) in groundwater contaminated with 60Co and 137Cs using ultrafiltration, solid phase extraction and fluorescence analysis. J. Environ. Radioact. 138, 331-340. [pdf]
  15. Montpellier, L. H., Siemann, S. (2013) Effect of pH on the catalytic function and zinc content of native and immobilized anthrax lethal factor. FEBS Lett. 587, 317-321. [pdf]
  16. Borraro, V., Riopel, R., Caron, F., Siemann, S. (2012) Laboratory study on the impact of pH and salinity on the fluorescence signal of Natural Organic Matter (NOM) relevant to groundwaters from a Canadian Shield sampling site. Water Qual. Res. J. Can. 47, 131-139. [pdf]
  17. Säbel, C. E., Carbone, R., Dabous, J. R., Lo, S. Y., Siemann, S. (2011) Preparation and characterization of cobalt-substituted anthrax lethal factor. Biochem. Biophys. Res. Commun. 416, 106-110. [pdf]
  18. Smith, S. R., Guerra, E., Siemann, S., Shepherd, J. L. (2011) Au dissolution during the anodic response of short-chain alkylthiols with polycrystalline Au electrodes. Electrochim. Acta 56, 8291-8298. [pdf]
  19. Säbel, C. E., St-Denis, S., Neureuther, J. M., Carbone, R., Siemann, S. (2010) Alkaline earth metals are not required for the restoration of the apoform of anthrax lethal factor to its holoenzyme state. Biochem. Biophys. Res. Commun. 403, 209-213. [pdf]
  20. Caron, F., Sharp-King, K., Siemann, S., Smith, D. S. (2010) Fluorescence characterization of the natural organic matter in deep ground waters from the Canadian Shield, Ontario, Canada. J. Radioanal. Nucl. Chem. 286, 699-705. [pdf]
  21. Säbel, C. E., Neureuther, J. M., Siemann, S. (2010) A spectrophotometric method for the determination of zinc, copper, and cobalt ions in metalloproteins using Zincon. Anal. Biochem. 397, 218-226. [pdf]
  22. Säbel, C. E., Shepherd, J. L., Siemann, S. (2009) A direct spectrophotometric method for the simultaneous determination of zinc and cobalt in metalloproteins using 4-(2-pyridylazo)resorcinol. Anal. Biochem. 391, 74-76. [pdf]
  23. Gardonio. D., Siemann, S. (2009) Chelator-facilitated chemical modification of IMP-1 metallo-β-lactamase and its consequences on metal binding. Biochem. Biophys. Res. Commun. 381, 107-111. [pdf]
  24. Siemann, S., Badiei, H. R., Karanassios, V., Viswanatha, T., Dmitrienko, G. I. (2006) 68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-β-lactamase. Chem. Commun., 532-534. [pdf]
  25. Ramsaywak, P. C., Labbé, G., Siemann, S., Dmitrienko, G. I., Guillemette, J. G. (2004) Molecular cloning, expression, purification and characterization of fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis – a novel class II A tetramer. Protein Expr. Purif. 37, 220-228. [pdf]
  26. Siemann, S., Schneider, K., Oley, M., Müller, A. (2003) Characterization of a tungsten-substituted nitrogenase isolated from Rhodobacter capsulatus. Biochemistry 42, 3846-3857. [pdf]
  27. Siemann, S., Clarke, A. J., Viswanatha, T., Dmitrienko, G. I. (2003) Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-b-lactamases. Biochemistry42, 1673-1683. [pdf]
  28. Siemann, S., Evanoff, D., Marrone, L., Clarke, A. J., Viswanatha, T., Dmitrienko, G. I. (2002) N-Arylsulfonyl hydrazones as inhibitors of IMP-1 metallo-b-lactamase. Antimicrob. Agents Chemother. 46, 2450-2457. [pdf]
  29. Siemann, S., Brewer, D., Clarke, A. J., Dmitrienko, G. I., Lajoie, G., Viswanatha, T. (2002) IMP-1 metallo-b-lactamase: effect of chelators and assessment of metal requirement by electrospray mass spectrometry. Biochim. Biophys. Acta1571, 190-200. [pdf]
  30. Dick, S., Siemann, S., Frey, H. E., Lepock, J. R., Viswanatha, T. (2002) Recombinant lysine:N6-hydroxylase: Effect of cysteine alanine replacements on structural integrity and catalytic competence. Biochim. Biophys. Acta 1594, 219-233. [pdf]
  31. Siemann, S., Schneider, K., Dröttboom, M., Müller, A. (2002) The Fe-only nitrogenase and the Mo nitrogenase from Rhodobacter capsulatus: A comparative study on the redox properties of the metal clusters present in the di-nitrogenase components. Eur. J. Biochem. 269, 1650-1661. [pdf]
  32. Siemann, S., Schneider, K., Behrens, K., Knöchel, A., Klipp, W., Müller, A. (2001) FeMo cofactor biosynthesis in a nifE-mutant of Rhodobacter capsulatus. Eur. J. Biochem. 268, 1940-1952. [pdf]
  33. Marrone, L., Siemann, S., Beecroft, M., Viswanatha, T. (1996) Specificity of lysine:N6-hydroxylase: A hypothesis for a reactive substrate intermediate in the catalytic mechanism. Bioorg. Chem. 24, 401-416. [pdf]

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