Publications

Selected Publications (MyBib Listing)

  • Nye, D.B., Johnson, E.A., Mai, M.H., and Lecomte, J.T.J.  Replacement of the heme axial lysine as a test of conformational adaptability in the truncated hemoglobin THB1. Journal of Inorganic Biochemistry, in press. doi:10.1016/j.jinorgbio.2019.110824
  • Nye, D.B. and Lecomte, J.T.J.  (2018) Replacement of the Distal Histidine Reveals a Non-Canonical Heme Binding Site in a 2-on-2 Hemoglobin.  Biochemistry, 57:5785–5796. doi:10.1021/acs.biochem.8b00752
  • Johnson, E.A., Russo, M.M., Nye, D.B., Schlessman, J.L., and Lecomte, J.T.J.  (2018) Lysine as a Heme Iron Ligand: A Property Common to Three Truncated Hemoglobins from Chlamydomonas reinhardtii.  Biochimica and Biophysica ActaGeneral Subjects, 1862:2660–2673.  doi:10.1016/j.bbagen.2018.08.009
  • Preimesberger, M.R., Johnson, E.A., Nye, D.B., and Lecomte, J.T.J.  (2017) Covalent Attachment of the Heme to Synechococcus Hemoglobin Alters Its Reactivity Toward Nitric Oxide.  Journal of Inorganic Biochemistry, 177:171–182.  doi:10.1016/j.jinorgbio.2017.09.018
  • Preimesberger, M.R., Majumdar, and Lecomte, J.T.J. (2017) Dynamics of Lysine as a Heme Axial Ligand: NMR Analysis of the Chlamydomonas reinhardtii Hemoglobin THB1. Biochemistry 56:551–569.  doi:10.1021/acs.biochem.6b00926
  • Johnson, E.A. and Lecomte, J.T.J. (2015) The Haemoglobins of Algae. Advances in Microbial Physiology 67:177–234. doi:10.1016/bs.ampbs.2015.08.003
  • Preimesberger, M.R., Majumdar, A., Rice, S.L., Que, L., and Lecomte, J.T.J. (2015) Helix-capping Histidines: Diversity of N-H…N Hydrogen Bond Strength Revealed by 2hJNN scalar couplings. Biochemistry 54:6896-908. doi:10.1021/acs.biochem.5b01002
  • Rice, S.L., Boucher, L.E., Schlessman, J.L., Preimesberger, M.R., Bosch, J., and Lecomte, J.T.J. (2015) Structure of Chlamydomonas reinhardtii THB1, a Group 1 Truncated Hemoglobin With a Rare Histidine-Lysine Heme Ligation. Acta Crystallographica Section F Structural Biology Communications 71:718–725. doi:10.1107/S2053230X15006949
  • Preimesberger, M.R., Majumdar, A., Aksel, T., Sforza, K., Lectka, T., Barrick, D., and Lecomte, J.T.J. (2015) Direct NMR Detection of Bifurcated Hydrogen Bonding in the α-Helix N-Caps of Ankyrin Repeat Proteins. Journal of the American Chemical Society 137:1008–1011. doi:10.1021/ja510784g
  • Johnson, E.A. and Lecomte, J.T.J. Characterization of the truncated hemoglobin THB1 from protein extracts of Chlamydomonas reinhardtii. F1000Research 3:294. doi:10.12688/f1000research.5873.1
  • Rice, S.L., Preimesberger, M.R., Johnson, E.A., and Lecomte, J.T.J. (2014) Introduction of a Covalent Histidine–Heme Linkage in a Hemoglobin: A Promising Tool for Heme Protein Engineering. Journal of Inorganic Biochemistry 141:198–207. doi:10.1016/j.jinorgbio.2014.09.009
  • Johnson, E.A., Rice, S.L., Preimesberger, M.R., Nye, D.B., Gilevicius, L., Wenke, B.B., Brown, J.M., Witman, G.B., and Lecomte, J.T.J. (2014) THB1, a Truncated Hemoglobin with Lysine as a Distal Heme Ligand, Is Linked to Nitrogen Metabolism in Chlamydomonas reinhardtii. Biochemistry 53:4573–4589. doi:10.1021/bi5005206
  • Wenke, B.B., Lecomte, J.T.J., Héroux, A., and Schlessman, J.L. (2014) The 2/2 Hemoglobin from the Cyanobacterium Synechococcus sp. PCC 7002 with Covalently Attached Heme: Comparison of X-ray and NMR structures. Proteins 82:528–534. doi:10.1002/prot.24409
  • Johnson, E.A. and Lecomte, J.T.J. The Globins of Cyanobacteria and Algae. Advances in Microbial Physiology 63:195–272. doi:10.1016/B978-0-12-407693-8.00006-6
  • Preimesberger, M.R., Wenke, B.B., Gilevicius, L., Pond, M.P., and Lecomte, J.T.J. (2013) Covalent Heme Attachment in Synechocystis Hemoglobin: Implications for Facile Histidine Posttranslational Modification. Biochemistry 52:3478–3488. doi:10.1021/bi400289e
  • Dellarole, M., Roumestand, C., Royer, C., and Lecomte, J.T.J. (2013) Volumetric Properties Underlying Ligand Binding In a Monomeric Hemoglobin: A High-Pressure NMR Study. Biochimica et Biophysica Acta 1834:1910–1922. doi:10.1016/j.bbapap.2013.04.016
  • Lecomte, J.T.J. and Falzone, C.J. (2013) Protein Structure: Unusual Covalent Bonds. Nature Encyclopedia of Life Sciences. doi:10.1002/9780470015902.a0003015.pub2
  • Pond, M.P., Majumdar, A., and Lecomte, J.T.J. (2012) Influence of Heme Post-Translational Modification and Distal Ligation on the Backbone Dynamics of a Monomeric Hemoglobin. Biochemistry 51:5733–5747. doi:10.1021/bi300624a
  • Pond, M.P., Wenke, B.B., Preimesberger, M.R., Rice, S.L., and Lecomte, J.T.J. (2012) 3-Fluorotyrosine as a Complementary Probe of Hemoglobin Structure and Dynamics: A 19F NMR Study of Synechococcus sp. PCC 7002 GlbN. Chemistry and Biodiversity 9:1703–1717. doi:10.1002/cbdv.201100448
  • Preimesberger, M.R., Pond, M.P., Majumdar, A., and Lecomte, J.T.J. (2012) Electron Self-Exchange and Self-Amplified Posttranslational Modification in the Hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002. Journal of Bioinorganic Chemistry 17:599-609. doi:10.1007/s00775-012-0880-5
  • Nothnagel, H.J., Winer, B.Y., Vuletich, D.A., Pond, M.P., and Lecomte, J.T.J. (2011) Structural Properties of 2/2 Hemoglobins: The Group III Protein from Helicobacter hepaticus. IUBMB Life 63:197–205 doi:10.1002/iub.430
  • Nothnagel, H.J., Preimesberger, M.R., Pond, M.P., Winer, B.Y., Adney, E.A., and Lecomte, J.T.J. (2011) Chemical Reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 Hemoglobins: Covalent Heme Attachment and Bishistidine Coordination. Journal of Biological Inorganic Chemistry 16:539–552. doi:10.1007/s00775-011-0754-2
  • Scott, N.L., Xu, Y., Shen, G., Vuletich, D.A., Falzone, C.J., Li, Z., Ludwig, M., Pond, M.P., Preimesberger, M.R., Bryant, D.A., and Lecomte, J.T.J. (2010) Functional and Structural Characterization of the 2/2 Hemoglobin from Synechococcus sp. PCC 7002. Biochemistry 49:7000–7011. doi:10.1021/bi100463d
  • Pond, M.P., Vuletich, D.A., Falzone, C.J., Majumdar, A., and Lecomte, J.T.J. (2009) 1H, 15N, and 13C Resonance Assignments of the 2/2 Hemoglobin from the Cyanobacterium Synechococcus sp. PCC 7002 in the Ferric Bis-histidine State. Biomolecular NMR Assignments 3:211–214. doi:10.1007/s12104-009-9177-1
  • Nothnagel, H.J., Love, N., and Lecomte, J.T.J. (2009) The Role of the Heme Distal Ligand in the Post-translational Modification of Synechocystis Hemoglobin. Journal of Bioinorganic Chemistry 103:107–116. doi:10.1016/j.jinorgbio.2008.09.009
  • Graham, J.E., Lecomte, J.T.J., and Bryant, D.A. (2008) Synechoxanthin: an Aromatic C40 Xanthophyll is a Major Carotenoid in the Cyanobacterium Synechococcus sp. PCC 7002. Journal of Natural Products 71:1647–1650. doi:10.1021/np800310b
  • Davis, R.B. Jr. and Lecomte, J.T.J. (2008) Structural Propensities in the Heme Binding Region of Apocytochrome b5. II. Heme Conjugates. Biopolymers–Peptide Science 90:556–566. doi:10.1002/bip.20995
  • Davis, R.B. Jr. and Lecomte, J.T.J. (2008) Structural Propensities in the Heme Binding Region of Apocytochrome b5. I. Free Peptides. Biopolymers–Peptide Science 90:544–555. doi:10.1002/bip.20996
  • Lecomte, J.T.J., Mukhopadhyay, K., and Pond, M.P. (2008) Structural and Thermodynamic Encoding in the Sequence of Rat Microsomal Cytochrome b5. Biopolymers 89:428–442. doi:10.1002/bip.20892
  • Landfried, D.A., Vuletich, D.A., Pond, M.P., and Lecomte, J.T.J. (2007) Structural and Thermodynamic Consequences of b Heme Binding for Monomeric Apoglobins and Other Apoproteins. Gene 398:12–28. doi:10.1016/j.gene.2007.02.046
  • Knappenberger, J.A., and Lecomte, J.T.J. (2007) Loop Anchor Modification Causes the Population of an Alternative Native State in an SH3-like Domain. Protein Science 16:863–879. doi:10.1110/ps.062469507
  • Vuletich, D.A., Falzone, C.J., and Lecomte, J.T.J. (2006) Structural and Dynamic Repercussions of Heme Binding and Heme-Protein Cross-Linking in Synechococcus sp. PCC 7002 Hemoglobin. Biochemistry 45:14075–14084. doi:10.1021/bi061532g
  • Knappenberger, J.A., Kuriakose, S.A., Vu, B.C., Nothnagel, H.J., Vuletich, D.A., and Lecomte, J.T.J. (2006) Proximal Influences in Two-on-Two Globins: Effect of the Ala69Ser Replacement on Synechocystis sp. PCC 6803 Hemoglobin. Biochemistry 45:11401–11413. doi:10.1021/bi060691x
  • Davis Jr, R.B., and Lecomte, J.T.J. (2006) A Dynamic N-cap Motif in Cytochrome b5. Evidence for a pH-controlled Conformational Switch. Proteins: Structure, Function, and Bioinformatics  63:336–348. doi:10.1002/prot.20759
  • Vuletich, D.A., and Lecomte, J.T.J. (2006) A Phylogenetic and Structural Analysis of Truncated Hemoglobins. Journal of Molecular Evolution 62:196–210. doi:10.1007/s00239-005-0077-4
  • Lecomte, J.T.J., Vuletich, D.A, and Lesk, A. M. (2005) Structural Divergence and Distant Relationships in Proteins: Evolution of the Globin Family. Current Opinion in Structural Biology 15:290–301. doi:10.1016/j.sbi.2005.05.008
  • Lecomte, J.T.J., Vu, B.C., and Falzone,C.J. (2005) Structural and Dynamic Properties of Synechocystis sp. PCC 6803 Hb Revealed by Reconstitution with Zn-Protoporphyrin IX. Journal of Inorganic Biochemistry 99:1585–1592. doi:10.1016/j.jinorgbio.2005.04.018
  • Moody, E.M., Lecomte, J.T.J., and Bevilacqua, P.C. (2005) Linkage Between Proton Binding and Folding in RNA: A thermodynamic framework and its experimental application for investigating pKa shifting. RNA 11:157–172. doi:10.1261/rna.7177505
  • Scott, N.L. and Lecomte, J.T.J. (2005) Protein Structure: Unusual Covalent Bonds. Nature Encyclopedia of Life Sciences John Wiley & Sons, Ltd: Chichester, UK (updated in 2013)
  • Knappenberger, J.A., Kraemer-Pecore, C.M., and Lecomte, J.T.J.(2004) Insertion of the Cytochrome b5 Heme-Binding Loop into an SH3 Domain. Effects on Structure and Stability, and Clues about the Cytochrome’s Architecture. Protein Science 13:2899–2908. doi:10.1110/ps.04902704.
  • Vu, B.C., Nothnagel, H.J., Vuletich, D.A., Falzone, C.J., and Lecomte, J.T.J. (2004) Cyanide Binding to Hexacoordinate Cyanobacterial Hemoglobins: Hydrogen Bonding Network and Heme Pocket Rearrangement in Ferric H117A Synechocystis Hb. Biochemistry 43:12622–12633. doi:10.1021/bi048726l
  • Mukhopadhyay, K. and Lecomte, J.T.J. (2004) A Relationship between Heme Binding and Protein Stability in Cytochrome b5. Biochemistry 43:12227–12236. doi:10.1021/bi0488956
  • Vu, B.C., Vuletich, D.A., Kuriakose, S.A., Falzone, C.J., and Lecomte, J.T.J. (2004) Characterization of the Heme-Histidine Cross-link in Cyanobacterial Hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002. Journal of Biological Inorganic Chemistry 9:183–194. doi:10.1007/s00775-003-0512-1
  • Kraemer-Pecore, C.M., Lecomte, J.T.J., and Desjarlais, J.R. (2003) A De Novo Redesign of the WW Domain. Protein Science 12:2194–2205. doi:10.1110/ps.03190903
  • Falzone, C.J., Vu, B.C., Scott, N.L., and Lecomte, J.T.J. (2002) The Solution Structure of the Recombinant Hemoglobin from the Cyanobacterium Synechocystis sp. PCC 6803 in its Hemichrome State. Journal of Molecular Biology 324:1015–1029. doi:10.1016/s0022-2836(02)01093-8
  • Vu, B.C., Jones, A.D., and Lecomte, J.T.J. (2002) Novel Histidine-Heme Covalent Linkage in a Hemoglobin. Journal of the American Chemical Society 124:8544–8545. doi:10.1021/ja026569
  • Scott, N.L., Falzone, C.J., Vuletich, D.A., Zhao, J., Bryant, D.A., and Lecomte, J.T.J. (2002) Truncated Hemoglobin from the Cyanobacterium Synechococcus sp. PCC 7002: Evidence for Hexacoordination and Covalent Adduct Formation in the Ferric Recombinant Protein. Biochemistry 22:6902–6910. doi:10.1021/bi025609m
  • Falzone, C.J. and Lecomte, J.T.J. (2002) Letter to the Editor: Assignment of the 1H, 13C, and 15N Signals of Synechocystis sp. PCC 6803 Methemoglobin. Journal of Biomolecular NMR 23:71–72.
  • Lee, K.K., Fitch, C.A., Lecomte, J.T.J., and García-Moreno E, B. (2002) Electrostatic Effects in Highly Charged Proteins: Salt Sensitivity of pKa Values of Histidines in Staphylococcal Nuclease. Biochemistry 41:5656–5667. doi:10.1021/bi0119417
  • Lecomte, J.T.J., Scott, N.L., Vu, B.C., and Falzone, C.J. (2001) Binding of Ferric Heme by the Recombinant Globin from the Cyanobacterium Synechocystis sp. PCC 6803. Biochemistry 40:6541–6552. doi:10.1021/bi010226u
  • Falzone, C.J., Wang, Y., Vu, B.C., Scott, N.L., Bhattacharya, S., and Lecomte, J.T.J. (2001) Structural and Dynamic Perturbations Induced by Heme Binding in Cytochrome b5. Biochemistry 40:4879–4891. doi:10.1021/bi002681g
  • Kao, Y.H., Fitch, C.A., Bhattacharya, S., Sarkisian, C.J., Lecomte, J.T.J., and García-Moreno E., B. (2000) Salt Effects on Ionization Equilibria of Histidines in Myoglobin. Biophysical Journal 79:1637–1654.
  • Scott, N.L and Lecomte, J.T.J. (2000) Cloning, Expression, Purification, and Preliminary Characterization of a Putative Hemoglobin from the Cyanobacterium Synechocystis sp. PCC 6803. Protein Science 9:587–597.
  • Mayer, K.L., Shen, G., Bryant, D.A., Lecomte, J.T.J., and Falzone, C.J. (1999) The Solution Structure of Photosystem I Accessory Protein E from the Cyanobacterium Nostoc sp. Strain PCC 8009. Biochemistry 38:13736–13746. doi:10.1021/bi9910373
  • Lecomte, J.T.J., Sukits, S.F., Bhattacharya, S., and Falzone, C.J. (1999) Conformational Properties of Native Sperm Whale Apomyoglobin in Solution. Protein Science 8:1484–1491.
  • Bhattacharya, S., Falzone, C.J., and Lecomte, J.T.J. (1999) The Backbone Dynamics of Apocytochrome b5 in Its Native, Partially Folded State. Biochemistry 38:2577–2589. doi:10.1021/bi995081u
  • Constans, A.J., Mayer, M.R., Sukits, S.F., and Lecomte, J.T.J. (1998) A Test of the Relationship between Sequence and Structure in Proteins: Excision of the Heme Binding Site in Apocytochrome b5. Protein Science 7:1983–1993.
  • Bhattacharya, S. and Lecomte, J.T.J. (1997) The Temperature Dependence of Histidine Ionization Constants in Myoglobin. Biophysical Journal 73:3241–3256.
  • Bhattacharya, S., Sukits, S.F., MacLaughlin, K.L, and Lecomte, J.T.J. (1997) The Tautomeric State of Histidines in Myoglobin. Biophysical Journal 73:3230–3240.
  • Falzone, C.J., Mayer, M.R., Whiteman, E.L., Moore, C.D., and Lecomte, J.T.J. (1996) Design Challenges for Hemoproteins: The Solution Structure of Apocytochrome b5. Biochemistry 35:6519–6526. doi:10.1021/bi960501q
  • Lecomte, J.T.J., Kao, Y.-H., and Cocco, M.J. (1996) The Native State of Apomyoglobin Described by Proton NMR Spectroscopy: The A-B-G-H Interface of Wild-Type Sperm Whale Apomyoglobin. Proteins: Structure Function and Genetics 25:267–285.
  • Falzone, C.J., Kao, Y.-H., Zhao, J., Bryant, D.A., and Lecomte, J.T.J. (1994) Three-Dimensional Solution Structure of PsaE from the Cyanobacterium Synechococcus sp. Strain PCC 7002: a Photosystem I Protein that Shows Structural Homology with SH3 Domains. Biochemistry 33:6052–6062.
  • Falzone, C.J., Kao, Y.-H., Zhao, J., MacLaughlin, K.L., Bryant, D.A., and Lecomte, J.T.J. (1994) 1H and 15N NMR Assignments of PsaE, a Photosystem I Subunit from the Cyanobacterium Synechococcus sp. Strain PCC 7002. Biochemistry 33:6043–6051.
  • Cocco, M.J. and Lecomte, J.T.J. (1994) The Native State of Apomyoglobin Described by Proton NMR Spectroscopy: Interaction with the Paramagnetic Probe HyTempo and the Fluorescent Dye ANS. Protein Science 3:267–281.
  • Kao, Y.-K. and Lecomte, J.T.J. (1993) Determination of the Zero-field Splitting Constant in Metaquomyoglobin for Proton NMR Chemical Shift Analysis. Structural Implications. Journal of the American Chemical Society 115:9754–9762.
  • Moore, C.D. and Lecomte, J.T.J. (1993) Characterization of an Independent Structural Unit in Apocytochrome b5. Biochemistry 32:199–207.
  • Cocco, M.J., Barrick, D., Taylor, S.V., and Lecomte, J.T.J. (1992) Histidine 82 Influences Heme Orientational Isomerism in Myoglobin. Long-range Effect Due to the Modification of a Conserved Residue. Journal of the American Chemical Society 114:11000–11001.
  • Cocco, M.J., Kao, Y.-H., Phillips, A.T., and Lecomte, J.T.J. (1992) Structural Comparison of Apomyoglobin and Metaquomyoglobin: pH Titration of Histidines by NMR Spectroscopy. Biochemistry 31:6481–6491.
  • Falzone, C.J., Benesi, A.J., and Lecomte, J.T.J. (1992) Characterization of Taxol in Methylene Chloride by NMR Spectroscopy. Tetrahedron Letters 33:1169–1172.
  • Lecomte, J.T.J. and Moore, C.D. (1991) Helix Formation in Apocytochrome b5: The Role of a Neutral Histidine at the N-Cap Position. Journal of the American Chemical Society 113:9663–9665.
  • Moore, C.D., Al-Misky, O.N., and Lecomte, J.T.J. (1991) Similarities in Structure between Holocytochrome b5 and Apocytochrome b5: NMR Studies of the Histidine Residues. Biochemistry 30:8357–8365.
  • Lecomte, J.T.J., Unger, S.W., and La Mar, G.N. (1991) Practical Considerations for the Measurement of the Homonuclear Overhauser Effect on Strongly Relaxed Protons in Paramagnetic Proteins. Journal of Magnetic Resonance 94:112–122.
  • Cocco, M.J. and Lecomte, J.T.J. (1990) Characterization of Hydrophobic Cores in Apomyoglobin: A Proton NMR Spectroscopy Study. Biochemistry 29:11067–11072.
  • Lecomte, J.T.J. and Cocco, M.J. (1990) Structural Features of the Protoporphyrin-Apomyoglobin Complex: A Proton NMR Spectroscopy Study. Biochemistry 29:11057–11067.
  • Moore, C.D. and Lecomte, J.T.J. (1990) Structural Properties of Apocytochrome b5: Presence of a Stable Native Core. Biochemistry 29:1984–1989.
  • Lecomte, J.T.J., Smit, J.D.G., Winterhalter, K., and La Mar, G.N. (1989) Structural and Electronic Properties of the Liver Fluke Hemoglobin Heme Cavity by Nuclear Magnetic Resonance and Optical Spectroscopy: Evidence for a Distal Tyrosine in a Normally Functioning Hemoglobin. Journal of Molecular Biology 209:235–246.
  • Emerson, S.D., Lecomte, J.T.J., and La Mar, G.N. (1989) 1H NMR Resonance Assignment and Dynamic Analysis of Phenylalanine CD1 in Low-Spin Ferric Complex of Sperm Whale Myoglobin. Journal of the American Chemical Society 110:4176–4182.
  • Lecomte, J.T.J. and La Mar, G.N. (1987) 1H NMR Probe for Hydrogen Bonding of Distal Residues to Bound Ligands in Heme Proteins: Isotope Effect on Heme Electronic Structure of Myoglobin. Journal of the American Chemical Society 109:7219–7220.
  • Lecomte, J.T.J., La Mar, G.N., Smit, J.D.G., Winterhalter, K.H., Smith, K.M., Langry, K.C., and Leung, H.- K. (1987) Structural and Electronic Properties of the Liver Fluke Hemoglobin Heme Cavity by Nuclear Magnetic Resonance: Heme Isotope Labeling. Journal of Molecular Biology 197:101–110.
  • Lecomte, J.T.J., Kaplan, D., Llinás, M., Thunberg, E., and Samuelsson, G. (1987) Proton Magnetic Resonance Characterization of Phoratoxins and Homologous Proteins Related to Crambin. Biochemistry 26:1187–1194.
  • Chatfield, M.J., La Mar, G.N., Lecomte, J.T.J., Balch, A.L., Smith, K.M., and Langry, K.C. (1986) Identification of the Altered Pyrrole in Sulfmyoglobin and an Extractable “Sulfhemin”: Participation of the 4-Vinyl Group in the Saturation of the Pyrrole in One of the Forms of Sulfmyoglobin. Journal of the American Chemical Society 108:7108–7110.
  • Pande, U., La Mar, G.N., Lecomte, J.T.J., Ascoli, F., Brunori, M., Smith, K.M., Pandey, R.K., Parish, D.W., and Thanabal, V. (1986) NMR Study of the Molecular and Electronic Structure of the Heme Aplysia Metmyoglobin. Resonance Assignment Based on Isotope Labeling and Proton Nuclear Overhauser Effect Measurements. Biochemistry 25:5863–5646.
  • La Mar, G.N., Emerson, S.D., Lecomte, J.T.J., Pande, U., Smith, K.M., Craig, G.W., and Kehres, L.A. (1986) The Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements. Journal of the American Chemical Society 108:5568–5573.
  • Chatfield, M.J., La Mar, G.N., Smith, K.M., Balch, A.L., and Lecomte, J.T.J. (1986) Multiple Forms of Sulfmyoglobin as Detected by Proton Nuclear Magnetic Resonance Spectroscopy. Biochemical and Biophysical Research Communications 135:309–315.
  • Lecomte, J.T.J. and La Mar, G.N. (1986) The Homonuclear Overhauser Effect in Water Solution of Low-Spin Hemeproteins: Assignment of Protons in the Heme Cavity of Sperm Whale Myoglobin. European Biophysics Journal 13:373–381.
  • Lecomte, J.T.J. and La Mar, G.N. (1985) Proton NMR Study of Labile Proton Exchange in the Heme Cavity as a Probe for the Potential Ligand Entry Channel in Myoglobin. Biochemistry 24:7388–7395.
  • Unger, S.W., Lecomte, J.T.J., and La Mar, G.N. (1985) The Utility of the Nuclear Overhauser Effect for Peak Assignment and Structure Elucidation in Paramagnetic Proteins. Journal of Magnetic Resonance 64:521–526.
  • Lecomte, J.T.J., Johnson, R.D., and La Mar, G.N. (1985) Characterization of Heme Orientational Disorder in Myoglobin by Nuclear Overhauser Effect. Biochimica et Biophysica Acta 829:268–274.
  • Lecomte, J.T.J., La Mar, G.N., Winterhalter, K.H., and Smit, J.D.G. (1984) Proton NMR Investigation of the Heme Cavity Structure of Liver Fluke (Dicrocœlium dendriticum) Methemoglobin. Journal of Molecular Biology 180:357–370.
  • Lecomte, J.T.J. and Llinás, M. (1984) Characterization of the Aromatic Proton Magnetic Resonance Spectrum of Crambin. Biochemistry 23:4799–4807.
  • Lecomte, J.T.J. and Llinás, M. (1984) Spectral Patterns of Rapidly Flipping Tyrosyl Rings, a Study of Crambin in Organic Solvents. Journal of the American Chemical Society 106:2741–2748.
  • Waddell, W.H.,Lecomte, J., West, J.L., and Younes, U.E. (1984) Qualitative Studies of the Low Temperature Photochemistry of Rhodopsin and Related Pigments. Photochemistry and Photobiology 39:213–219.
  • Lecomte, J.T.J., Jones, B.L., and Llinás, M. (1982) Proton Magnetic Resonance Studies of Barley and Wheat Thionins: Structural Homology with Crambin. Biochemistry 21:4843–4849.
  • Lecomte, J.T.J., De Marco, A., and Llinás, M. (1982) Analysis of the Methyl Proton NMR Spectrum of Crambin, a Hydrophobic Protein. Biochimica et Biophysica Acta 703:223–230.
  • De Marco, A., Lecomte, J.T.J., and Llinás, M. (1981) Solvent and Temperature Effects on Crambin, a Hydrophobic Protein, as Investigated by Proton Magnetic Resonance. European Journal of Biochemistry 119:483–490.
  • Llinás, M. and Lecomte, J.T.J. (1980) Solvent and Temperature Effects on Crambin, a Hydrophobic Protein. Biophysical Journal 32:90–91.
  • Llinás, M., De Marco, A., and Lecomte, J.T.J. (1980) Proton Magnetic Resonance of Crambin, a Hyperstable Hydrophobic Protein, at 250 and 600 MHz. Biochemistry 19:1140–1145.
  • Piette, J.-L., Lecomte, J.T.J., and Lecomte, J. (1978) Propriétés Convulsivantes de Quelques Dérivés Organo-Séléniés. Comptes Rendus des Séances de la Société de Biologie 172:383–387.
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