Publications

List of selected publications: 

  • Piazza, M., Dieckmann, T., Guillemette, J.G. 2016, Structural Studies of a Complex between endothelial Nitric Oxide Synthase and Calmodulin at Physiological Calcium Concentration. Biochemistry 55, 5962-5971.  
  • Piazza, M., Guillemette, J.G., Dieckmann, T. 2016. Chemical shift assignments of calmodulin constructs with EF hand mutations. Biomol. NMR Assign. 10, 193-198.
  • Blondeel, E.J.M., Ho, R., Schulze, S., Sokolenko, S., Guillemette, S., Slivac, I., Durocher, Y., Guillemette, J.G., McConkey, B., Chang, D., Aucoin, M.G. 2016, An Omics Approach to Rational Feed: Enhancing Growth in CHO Cultures with NMR Metabolomics and 2D-DIGE Proteomics. J. of Biotechnology 234, 127-138.
  • Piazza, M., Guillemette, J.G., Dieckmann, T. 2015. Dynamics of nitric oxide synthase-calmodulin interactions at physiological calcium concentrations. Biochemistry. 54, 1989-2000.
  • Piazza, M., Guillemette, J.G., Dieckmann, T. 2015. Chemical shift perturbations induced by residue specific mutations of CaM interacting with NOS peptides. Biomol NMR Assign. 9, 299-302.
  • Piazza, M., Taiakina, V., Guillemette, S.R. Guillemette, J.G., Dieckmann, T 2014, Solution structure of calmodulin bound to the target peptide of endothelial nitric oxide synthase phosphorylated at Thr495. Biochemistry 53, 1241-1249.
  • Astashkin, A.V.,Chen, L., Zhou, X., Li, H., Poulos, T.L., Liu, K.J., Guillemette, J.G., Feng, C. 2014. Pulsed electron paramagnetic resonance study of domain docking in neuronal nitric oxide synthase: the calmodulin and output state perspective. J. Phys. Chem. A. 118, 6864-6872.
  • Taiakina, V., Boone, A.N., Fux, J., Senatore, A., Weber-Adrian, D., Guillemette, J.G., Spafford, J.D. 2013, The calmodulin-binding, short linear motif, NSCaTE is conserved in L-type channel ancestors of vertebrate Cav1.2 and Cav1.3 channels. PloS one. 8(4): e61765.
  • Astashkin, A.V., Elmore, B.O., Chen, L., Fan, W., Guillemette, J.G., Feng, C. 2012, Pulsed ENDOR Determination of the Arginine Location in the Ferrous-NO Form of Neuronal NOS,  J. Phys. Chem. A. 116, 6731-6739.
  • Crawford, B., Koshy, S.T., Jhamb, G., Woodford, C., Thompson, C.M., Levy, A.S., Rush, J.W.E., Guillemette, J.G., Lillicrap, D., Jervis J. 2012, Cardiac Decellularisation With Long-Term Storage and Repopulation With Canine Peripheral Blood Progenitor Cells. Can. J. Chem. Eng. 90, 1457-1464.
  • Piazza, M., Futrega, K., Spratt, D.E., Dieckmann, T., Guillemette, J.G. 2012, Structure and dynamics of calmodulin (CaM) bound to nitric oxide synthase peptides: effects of a phosphomimetic CaM mutation. Biochemistry. 51, 3651−3661.
  • Li, W., Fan, W., Chen, L., Elmore, B.O., Piazza, M., Guillemette, J.G., Feng, C. 2012, Role of an isoform specific serine residue in FMN-heme electron transfer in inducible nitric oxide synthase. J. Biol. Inorg. Chem. 17, 675-685.
  • Labbé, G., Krismanich, A.P., de Groot, S., Rasmusson, T., Shang, M., Brown, M.D., Dmitrienko, G.I., Guillemette, J.G. 2012, Development of metal-chelating inhibitors for the Class II fructose 1,6-bisphosphate (FBP) aldolase. J. Inorg. Biochem. 112: 49-58.
  • Piazza , M., Duangkham, Y., Spratt, D.E., Dieckmann, T. and Guillemette. J.G. 2011,  Expression and purification of an isotopically labeled aggregation prone iNOS CaM-binding protein for use in NMR studies. J. Label. Comp. and Radiopharm 54, 657–663.
  • Spratt, D.E., Duangkham, Y., Taiakina, V. and Guillemette, J.G. 2011, Mapping the binding and CaM-dependent activation of NOS isozymes. The Open Nitric Oxide J. 3, 15-23.
  • Labbé, G., de Groot, S., Rasmusson, T., Milojevic, G., Dmitrienko, G.I. and Guillemette, J.G. 2011, Evaluation of Four Microbial Class II fructose 1,6-bisphosphate aldolase enzymes for use as biocatalysts, Protein Expr. Purif. 80, 224-233.
  • Feng, C., Ghosh, D.K., Taiakina, V., Guillemette, J. G., Tollin, G. 2011, Intraprotein electron transfer between the FMN and heme domains in endothelial nitric oxide synthase holoenzyme, Biochimica et Biophysica Acta, 1814, 1997-2002.
  • Crawford B., Koshy S., Jhamb G., Woodford C., Thompson C. M., Levy A. S., Rush J. W. E., Guillemette J. G., Lillicrap D., Jervis E. 2012, Process Engineering Considerations for Cardiac Decellularization, Can. J. Chem. Eng. 90, 1457-1464.
  • Sempombe, J., Galinato, M.G.I., Elmore, B.O., Fan, W., Guillemette, J.G., Lehnert, N., Kirk, M.L., Feng, C. 2011, Mutation in the FMN Domain Modulates MCD Spectra of the iNOS Ferric Cyano Complex in a Substrate-Specific Manner, Inorganic Chemistry, 50, 6859- 61. 
  • Astashkin, A., Fan, W., Bradley, E., Guillemette, J. G., Feng, C. 2011, Pulsed ENDOR determination of relative orientation of g- and molecular-frames of imidazole-coordinated heme center of NOS, J. Phys. Chem., 115, 10345-10352. 
  • Feng, C., Fan, W., Dupont, A., Guillemette, J. G., Ghosh, D.K., Tollin, G. 2010,  Electron transfer in a human inducible NOS oxygenase/FMN construct coexpressed with the N- terminal globular domain of CaM. FEBS Letters 584,4335-4338. 
  • Astashkin, A.V., Elmore, B.O., Fan, W., Guillemette, J.G., and Feng, C. 2010, Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase. J Am Chem Soc. 132,12059-12067.
  • Montogmery, H.J., Dupont, A.L., Leivo, H.E. and Guillemette, J.G 2010, Cloning, Expression and Characterization of a Nitric Oxide Synthase-Like Protein from Bacillus cereus. Biochemistry Research International 2010:489892.
  • Sempombe, J., Elmore, B.O., Dupont, A, Ghosh, D., Guillemette, J.G., Kirk, M., and Feng C. 2009, Mutations in the FMN domain modulate MCD spectra of the heme site in the oxygenase domain of iNOS. J. Am. Chem. Soc. 131, 6940-6942.
  • Feng, C., Dupont, A.L., Spratt, D.E., Weinberg, J.B., Guillemette, J.G., Tollin, G., and Ghosh, D.K. 2009, Intraprotein Electron Transfer in Inducible Nitric Oxide Synthase Holoenzyme. Journal of Biological Inorganic Chemistry 14, 133-142
  • Spratt, D.E., Taiakina, V., Palmer, M., and Guillemette, J.G. 2008, FRET conformational analysis ofcalmodulin binding to nitric oxide synthase peptides and enzymes. Biochemistry, 47, 12006-12017.
  • Spratt, D.E., Israel, O.K., Taiakina, V., and Guillemette, J.G. 2008, Regulation of inducible nitric oxidesynthase by electrostatic interactions in the linker region of calmodulin. Biochimica et Biophysica Acta, 1784, 2065-2070.
  • Spratt, D.E., Taiakina, V., Palmer, M. and Guillemette, J.G. 2007, Differential Binding of Calmodulin Domains to Constitutive and Inducible Nitric Oxide Synthase Enzymes, Biochemistry 46, 8288-8300.
  • Spratt, D.E., Taiakina, V. and Guillemette, J.G. 2007, Calcium-deficient calmodulin binding and activation of neuronal and inducible nitric oxide synthases. Biochim Biophys Acta. 1774, 1351-1358.
  • Labbé, G., Bezaire, J., de Groot, S. How, C., Rasmusson, T., Yaeck, J., Jervis, J., Dmitrienko , and G.I., Guillemette, J.G. 2007, High level production of the Magnaporthe grisea Fructose 1,6-bisphosphate Aldolase enzyme in E. coli using a small volume Bench Top Fermentor, Protein Expr. Purif. 51, 110-119.
  • Feng, C., Tollin, G., Hazzard, J.T., Nahm, N.J., Guillemette, J.G., Salerno, J.C. and Ghosh, D.K. 2007, Direct measurement by laser flash photolysis of intraprotein electron transfer in a rat neuronal nitric oxide synthase. J Am Chem Soc. 129, 5621-5629.
  • Spratt, D.E., Newman, E., Mosher, J. Ghosh, D.K., Salerno, J.C. and Guillemette, J.G. 2006, Binding and Activation of Nitric Oxide Synthase isozymes by Calmodulin EF Hand Pairs. FEBS journal 273, 1759-1771.
  • Lang, S., Spratt, D.E., Guillemette, J.G., and Palmer, M. 2006 Selective labeling of selenomethionine residues in proteins with a fluorescent derivative of benzyl bromide. Anal. Biochem. 359, 253-258.
  • Perdicakis, B.S., Montgomery, H.J., Abbott GL, Fishlock D, Lajoie GA, Guillemette, J.G. and Jervis, E. 2005, Photo-Control of Nitric Oxide Production in Cell Culture Using a Caged Isoform Selective Inhibitor. Bioorg. Med. Chem. 13, 47-57.
  • Perdicakis, B., Montgomery, H.J., Guillemette, J.G. and  Jervis, E. 2005, Analysis of slow-binding  enzyme inhibitors at elevated enzyme concentrations Anal. Biochem. 337, 211-223.
  • Lang, S., Spratt, D.E., Guillemette, J.G. 2005, Dual-targeted labeling of proteins using cysteine and selenomethionine residues. Anal. Biochem. 342, 271-279.
  • Ahmed V., Ispahany M., Ruttgaizer S., Guillemette J.G., Taylor S.D. 2005, A fluorogenic substrate for the continuous assaying of aryl sulfatases. Anal. Biochem, 340, 80-88.
  • Newman, E., Spratt, D.E., Mosher, J., Cheyne, B.,  Montgomery, H.J., Wilson, D.L., Weinberg, J.B., Smith, S.M.E., Salerno, J.C., Ghosh, D.K.,  and Guillemette, J.G.  2004, Differential activation of nitric oxide synthase isozymes by calmodulin-troponin C chimeras. J. Biol. Chem., 279, 33547-33557.
  • Ramsaywak,P.C.,Labbé,G .,Sieman,S.,Dmitrienko,G.I.and Guillemette,J.G. 2004, Molecular cloning, expression, purification and characterization of Fructose-1,6-bisphosphate aldolase from Mycobacterium tuberculosis – a novel class II tetramer. Protein Expr. Purif. 37, 220-228.
  • Gao,Y.T.,Smith,S.M.,Weinberg,J.B., Montgomery,H.J., Newman,E., Ghosh,K., Guillemette,J.G.and Salerno, J.C. 2004, Thermodynamics of oxidation-reduction reactions in mammalian nitric oxide synthase isoforms J.Biol.Chem 279, 18759-18766.
  • Lapierre,J .,Ahmed,V.,Chen,M.J.,Ispahany M., Guillemette,J.G.and Taylor,S.D. 2004, The difluoromethylene group as a replacement for the labile oxygen in steroid sulfates:A new approach to steroid sulfatase inhibitors. Bioorg Med Chem Lett. 14, 151-155.
  • Perdicakis B, Montgomery HJ, Guillemette JG and  Jervis E. 2004, Validation and characterization of uninhibited enzyme kinetics performed in multiwell plates. Anal. Biochem. 332, 122-136.
  • Montgomery, H. J., Bartlett, R., Pediacakis, B., Squier, T., Jervis, E. and Guillemette, J. G. 2003, Activation of Constitutive Nitric Oxide Synthases by Oxidized Calmodulin Mutants. Biochemistry 42, 7759-7768.
  • Acchione, M., Guillemette, J. G. Twine, S.M., Hogue, C.W.W., Rajendran, B., Szabo, A.G. 2003, Fluorescence Based Structural Analaysis of Tryptophan Analogue-AMP Formation in Single Tryptophan Mutants of B. stearothermophilus Tryptophanyl-tRNA Synthetase. Biochemistry 42, 14994-15002.
  • Fishlock, D., Montgomery, H.J., Perdicakis, B.,  Jervis, E., Guillemette, J.G. and Lajoie, G. 2003, Synthesis And Evaluation Of trans 3,4-Cyclopropyl L-Arginine Analogs as Isoform Selective Inhibitors of Nitric Oxide Synthase.  Bioorganic & Med. Chem. 11, 869-873.
  • Lett, C.M. and Guillemette J.G., 2002, Increasing the Redox Potential of Iso-1-Cytochrome c Through the Modification of Select Heme Interactions. Biochem. J. 362, 281-287.
  • Blouin, C., Guillemette, J.G. and Wallace, C.J.A., 2002, Probing Electrostatic Interactions in Cytochrome c Using Site-Directed Mutagenesis. Biochem Cell Biol. 80, 197-203.
  • Montgomery, H.J., Perdicakis, B., Fishlock, D., Lajoie, G., Jervis, E. and Guillemette, J.G., 2002, Photo-Control of Nitric Oxide Synthase Activity Using a Caged Isoform Specific Inhibitor. Bioorganic & Med. Chem. 10, 1919-1927.
  • Fernando, P., Abdulee, R., Mohindra, A., Guillemette, J.G. and Heikkila, J.J. 2002, Mutation or Deletion of the C-terminal Tail Affects the Function and Structure of Xenopus laevis Small Heat Shock Protein, hsp30. Comparative Biochemistry and Physiology Part B 133, 95-103.
  • Fislock, D., Guillemette, J.G. and Lajoie, G., 2002, Synthesis of Syn and Anti Isomers of Trans-Cyclopropyl Arginine J. Org. Chem. 67, 2352-2354. 
  • Blouin, C., Guillemette, J.G., and Wallace C.J.A., 2001, Resolving the Individual Components of a pH-Induced Conformational Change. Biophys. J. 81, 2331-2338.
  • Parrish, J.C., Guillemette, J.G. and Wallace, C.J.A., 2001, Contribution of Leucine 85 to the Structure and Function of S. Cerevisiae iso-1 Cytochrome c. Biochem Cell Biol. 79, 517-524. 
  • Parrish, J.C., Guillemette, J.G. and Wallace, C.J.A., 2001, A tale of two charges; distinct roles for an acidic and a basic amino acid in the structure and function of cytochrome c. Biochem. Cell. Biol. 79, 83-91.
  • Montgomery, H.J., Romanov, V. and Guillemette, J.G., 2000, Removal of a Putative Inhibitory Element Reduces the Ca2+-Dependent Calmodulin Activation of Neuronal Nitric Oxide Synthase. J. Biol. Chem. 275, 5052-5058.
  • Feinberg, B.A., Guillemette, J.G., Frey, H.E., Smirl, T.N., and Margoliash, E., 2000, A calorimetric study of the rat cytochome c Tyr-67-Phe variant. The Chemist 77, 11-18.
  • Noble, M.A., Munro, A.W., Rivers, S.L. Robeldo, L., Daff, S.M., Yellowlees, L.J., Shimizu, T., Sagami, I., Guillemette, J.G., and Chapman, S.K., 1999, Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.  Biochemistry 38, 16413-16418.
  • Lett, C.M., Rosu-Myles, M.D., Frey, H.E. and Guillemette, J. G. 1999, Rational design of a more stable yeast iso-1-cytochrome c, Biochim. Biophys. Acta 1432, 40-48.
  • Mombelli., E., Lange, R., Kornblatt, J. and Kornblatt, J.A. Guillemette, J.G., 1999, Individual tyrosines of proteins: their spectra may or may not differ from those in water or other solvents, Biochem. Biophys. Acta 1431, 238-248.
  • Newton, D.C., Montgomery, H.J. and J.G. Guillemette, 1998, The Reductase Domain of the Human Inducible Nitric Oxide Synthase Is Fully Active in the Absence of Bound Calmodulin, Archiv. Biochem. Biophys. 359, 249-257. 
  • Schroeder, H.R., McOdimba, F.A., GuillemetteJ.G. and. Kornblatt. J.A 1997, The Polarity of Tyrosine 67 in Yeast Iso-1-Cytochrome c Monitored by Second Derivative Spectroscopy, Biochem. Cell. Biology 75, 191-197.
  • Lett, C.M., Berghuis, A.M., Frey, H.E., Lepock, J.R., Guillemette, J.G. 1996, The role of a conserved water molecule in the redox dependent thermal stability of iso-1-cytochrome c, J. Biol. Chem. 271, 29088-29093. 
  • Woods, A.C., Guillemette, J. G., Parrish, J.C., Smith, M., Wallace, C.J.A. 1996 Synergy in protein engineering: mutagenic manipulation of protein structure to simplify semisynthesis. J. Biol. Chem. 271, 32008-32015.
  • Rafferty, S.P., Guillemette, J.G., Berghuis, A.M., Smith, M., Brayer, G.D., and Mauk, A.G. 1996. Mechanistic and structural contributions of critical surface and internal residues to cytochrome c electron transfer reactivity.Biochemistry 35, 10784-10792.
  • Keyvani-Amineh, H., Guillemette, J.G., Diouri, M., and Weber, J.M.. 1995. Electrophoretic and Spectral Characterisation of Wild Type and Mutant Adenovirus Protease. J. Biol. Chem. 270, 23250-23253.
  • Lo, T.P., Guillemette, J. G., Louie, G.V., Smith, M. and Brayer, G.D. 1995a. Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome c, Biochemistry 34, 163-171.
  • Lo, T.P., Murphy, M.E.P., Guillemette, J.G., Smith, M., and Brayer, G.D. 1995b. Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c. Protein Science 4, 198-208.
  • Guillemette, J.G., Barker, P.D., Eltis, L.D., Lo, T.P. Brayer, G.D. Mauk, A.G. and Smith, M. 1994. Analysis of the bimolecular reduction of ferricytochrome cby Ferrocytochrome b5 through mutagenesis and molecular modeling. Biochimie 76, 592-604.
  • Huang, Y., Beeser, S., Guillemette, J.G., Stroms, R.K. and Kornblatt, J.A. 1994 The Inhibition of electron transfer activity of cytochrome c by a cross-link on the protein surface. Eur. J. Biochemistry 223, 155-160.
  • Berghuis, A. M., Guillemette, J. G., Mauk, A. G., Brayer, G. D. and Smith, M. 1994a Mutation of the Conserved Tyrosine Residue at Position 67 Significantly Modifies the Heme Environment in Yeast Iso-1-cytochrome c.  J. Mol. Biol. 235, 1326-1341.
  • Berghuis, A. M., Guillemette, J. G., McLendon, G., Sherman, F., Smith, M. and Brayer, G.D. 1994b The Role of a Conserved Internal Water Molecule and its Associated Hydrogen Bond Network in Cytochrome c. J. Mol. Biol. 236, 786-799.
  • Ferrer, J.C., Guillemette, J.G., Bogumil, R., Inglis, S.V., Smith, M., and Mauk, A.G. 1993 Identification of Lys79 as an Iron Ligand in One Form of Alkaline Yeast Iso-1-Ferricytochrome c. J. Am. Chem. Soc. 115, 7507-7508.
  • Davies, A. M., Guillemette, J. G., Smith, M., Greenwood, C., Thurgood, G. P., Mauk, A. G. and Moore, G. R. 1993 Assessment of the Functional and Spectroscopic Contributions of the Environment of Cytochrome c Heme Propionate-7. Biochemistry 32, 5431-5435.
  • Northrop, S. H., Thomasson, K. A., Miller, C. M., Eltis, L. D., Barker, P. D., Guillemette, J. G., Inglis, S.C., Mauk, A. G. 1993 Effects of Charged Amino Acid Mutations on the Bimolecular Kinetics of Reduction of Yeast iso-1-Ferricytochrome c by Bovine Ferrocytochrome b5. Biochemistry32, 6613-6623.

Last updated November 24, 2016