{"id":7,"date":"2013-09-10T12:21:41","date_gmt":"2013-09-10T12:21:41","guid":{"rendered":"https:\/\/sites.krieger.jhu.edu\/template-research\/?page_id=7"},"modified":"2025-09-25T15:54:15","modified_gmt":"2025-09-25T15:54:15","slug":"publications","status":"publish","type":"page","link":"https:\/\/sites.krieger.jhu.edu\/lecomte-lab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"<p>Selected Publications (<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/sites\/myncbi\/juliette.lecomte.1\/collections\/47412619\/public\/\">MyBib<\/a> Listing)<\/p>\n<ul>\n<li>Martinez Grundman, J.E., Schultz, T.D., Schlessman, J.L., Johnson, E. A., Gillilan, R.E., and Lecomte, J.T.J. (2025) Extremophilic Hemoglobins: The Structure of <em>Shewanella benthica<\/em> Truncated Hemoglobin N.\u00a0 <em>Journal of Biological Chemistry,<\/em>\u00a0<strong>301<\/strong>:108223.\u00a0 <a href=\"https:\/\/doi.org\/10.1016\/j.jbc.2025.108223\">doi:10.1016\/j.jbc.2025.108223<\/a><\/li>\n<li>Martinez Grundman, J.E., Schultz, T.D., Schlessman, J.L., Liu, K., Johnson, E.A., and Lecomte, J.T.J.\u00a0 (2024) Heme <em>d<\/em> Formation in a <em>Shewanella benthica<\/em> Hemoglobin. <em>Journal of Inorganic Biochemistry, <\/em><strong>259:<\/strong>112654.\u00a0<a href=\"https:\/\/doi.org\/10.1016\/j.jinorgbio.2024.112654\">doi:10.1016\/j.jinorgbio.2024.112654<\/a><\/li>\n<li>Lecomte, J.T.J., and Johnson, E.A.\u00a0 (2024) The Globins of Cyanobacteria and Green Algae: An Update. <em>Advances in Microbial Physiology, <\/em>Vol. 85<em>.<\/em>\u00a0<a href=\"https:\/\/doi.org\/10.1016\/bs.ampbs.2024.04.004\">doi:10.1016\/bs.ampbs.2024.04.004<\/a><\/li>\n<li>Martinez Grundman, J.E., Johnson, E.A., and Lecomte, J.T.J.\u00a0 (2023) Architectural Digest: Thermodynamic Stability and Domain Structure of a Consensus Monomeric Hemoglobin. <em>Biophysical Journal<\/em>, <strong>122<\/strong>:3117-3132. <a href=\"https:\/\/doi.org\/10.1016\/j.bpj.2023.06.016\">doi:10.1016\/j.bpj.2023.06.016<\/a><\/li>\n<li>Juli\u00f3 Plana, L., Martinez Grundman, J.E., Estrin, D.A., Lecomte, J.T.J., and Capece, L. (2021) Distal lysine (De)coordination in the Algal Hemoglobin THB1: A Combined Computer Simulation and Experimental Study. <em>Journal of Inorganic<\/em> <em>Biochemistry<\/em>, <strong>220<\/strong>:111455. <a href=\"https:\/\/doi.org\/10.1016\/j.jinorgbio.2021.111455\">doi:10.1016\/j.jinorgbio.2021.111455<\/a><\/li>\n<li>Martinez Grundman, J.E., Juli\u00f3 Plana, L., Schlessman, J.L., Capece, L., Estrin, D.A., and Lecomte, J.T.J. (2021) Control of Distal Lysine Coordination in a Monomeric Hemoglobin: A role for heme peripheral interactions. <em>Journal of Inorganic<\/em> <em>Biochemistry<\/em>, <strong>219:<\/strong>111437.\u00a0 <a href=\"https:\/\/doi.org\/10.1016\/j.jinorgbio.2021.111437\">doi:10.1016\/j.jinorgbio.2021.111437<\/a><\/li>\n<li>Lecomte, J.T.J. (2020) Hemoglobin: Some (Dis)Assembly Required.\u00a0 <em>Biophysical Journal<\/em>,\u00a0 <span class=\"docsum-journal-citation full-journal-citation\"><strong>118<\/strong>:1235-1237. <a href=\"https:\/\/doi.org\/10.1016\/j.bpj.2019.12.041\">doi:10.1016\/j.bpj.2019.12.041<\/a><\/span><\/li>\n<li>Nye, D.B., Johnson, E.A., Mai, M.H., and Lecomte, J.T.J.\u00a0 (2019) Replacement of the heme axial lysine as a test of conformational adaptability in the truncated hemoglobin THB1. <em>Journal of Inorganic<\/em> <em>Biochemistry<\/em>, 110824. <a href=\"https:\/\/doi.org\/10.1016\/j.jinorgbio.2019.110824\">doi:10.1016\/j.jinorgbio.2019.110824<\/a><\/li>\n<li>Nye, D.B. and Lecomte, J.T.J.\u00a0 (2018) Replacement of the Distal Histidine Reveals a Non-Canonical Heme Binding Site in a 2-on-2 Hemoglobin.\u00a0 <em>Biochemistry<\/em>, <strong>57<\/strong>:5785\u20135796. <a href=\"https:\/\/dx.doi.org\/10.1021\/acs.biochem.8b00752\">doi:10.1021\/acs.biochem.8b00752<\/a><\/li>\n<li>Johnson, E.A., Russo, M.M., Nye, D.B., Schlessman, J.L., and Lecomte, J.T.J.\u00a0 (2018) Lysine as a Heme Iron Ligand: A Property Common to Three Truncated Hemoglobins from <em>Chlamydomonas reinhardtii.\u00a0 Biochimica and Biophysica Acta<\/em> \u2013 <em>General Subjects<\/em>, <strong>1862<\/strong>:2660\u20132673.\u00a0 <a href=\"http:\/\/dx.doi.org\/10.1016\/j.bbagen.2018.08.009\">doi:10.1016\/j.bbagen.2018.08.009<\/a><\/li>\n<li>Preimesberger, M.R., Johnson, E.A., Nye, D.B., and Lecomte, J.T.J.\u00a0 (2017) Covalent Attachment of the Heme to <em>Synechococcus<\/em> Hemoglobin Alters Its Reactivity Toward Nitric Oxide.\u00a0 <em>Journal of Inorganic Biochemistry<\/em>, 177:171\u2013182.\u00a0 <a href=\"http:\/\/dx.doi.org\/10.1016\/j.jinorgbio.2017.09.018\">doi:10.1016\/j.jinorgbio.2017.09.018<\/a><\/li>\n<li>Preimesberger, M.R., Majumdar, and Lecomte, J.T.J. (2017) Dynamics of Lysine as a Heme Axial Ligand: NMR Analysis of the <em>Chlamydomonas reinhardtii<\/em> Hemoglobin THB1. <em>Biochemistry <\/em><strong>56<\/strong>:551\u2013569.\u00a0 <a href=\"http:\/\/dx.doi.org\/10.1021\/bi100463d\">doi:10.1021\/acs.biochem.6b00926<\/a><\/li>\n<li>Johnson, E.A. and Lecomte, J.T.J. (2015) The Haemoglobins of Algae. <em>Advances in Microbial Physiology<\/em> <strong>67<\/strong>:177\u2013234. <a href=\"http:\/\/dx.doi.org\/10.1016\/bs.ampbs.2015.08.003\">doi:10.1016\/bs.ampbs.2015.08.003<\/a><\/li>\n<li>Preimesberger, M.R., Majumdar, A., Rice, S.L., Que, L., and Lecomte, J.T.J. (2015) Helix-capping Histidines: Diversity of N-H&#8230;N Hydrogen Bond Strength Revealed by <sup>2h<\/sup><em>J<\/em><sub>NN<\/sub> scalar couplings. <em>Biochemistry<\/em> <strong>54<\/strong>:6896-908. <a href=\"http:\/\/dx.doi.org\/10.1021\/acs.biochem.5b01002\">doi:10.1021\/acs.biochem.5b01002<\/a><\/li>\n<li>Rice, S.L., Boucher, L.E., Schlessman, J.L., Preimesberger, M.R., Bosch, J., and Lecomte, J.T.J. (2015) Structure of <em>Chlamydomonas reinhardtii<\/em> THB1, a Group 1 Truncated Hemoglobin With a Rare Histidine-Lysine Heme Ligation. <em>Acta Crystallographica Section F Structural Biology Communications<\/em> <strong>71<\/strong>:718\u2013725. <a href=\"http:\/\/doi:10.1107\/S2053230X15006949\">doi:10.1107\/S2053230X15006949<\/a><\/li>\n<li>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 \u03b1-Helix N-Caps of Ankyrin Repeat Proteins. <em>Journal of the American Chemical Society<\/em> <strong>137<\/strong>:1008\u20131011. <a href=\"http:\/\/dx.doi.org\/10.1021\/ja510784g\">doi:10.1021\/ja510784g<\/a><\/li>\n<li>Johnson, E.A. and Lecomte, J.T.J. Characterization of the truncated hemoglobin THB1 from protein extracts of <em>Chlamydomonas reinhardtii<\/em>. <em>F1000Research<\/em> <strong>3<\/strong>:294. <a href=\"http:\/\/dx.doi.org\/10.12688\/f1000research.5873.1\">doi:10.12688\/f1000research.5873.1<\/a><\/li>\n<li>Rice, S.L., Preimesberger, M.R., Johnson, E.A., and Lecomte, J.T.J. (2014) Introduction of a Covalent Histidine\u2013Heme Linkage in a Hemoglobin: A Promising Tool for Heme Protein Engineering. <em>Journal of Inorganic Biochemistry<\/em> <strong>141<\/strong>:198\u2013207. <a href=\"http:\/\/dx.doi.org\/10.1016\/j.jinorgbio.2014.09.009\">doi:10.1016\/j.jinorgbio.2014.09.009<\/a><\/li>\n<li>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<em> Chlamydomonas reinhardtii<\/em>. <em>Biochemistry<\/em> <strong>53<\/strong>:4573\u20134589. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi5005206\">doi:10.1021\/bi5005206<\/a><\/li>\n<li>Wenke, B.B., Lecomte, J.T.J., H\u00e9roux, A., and Schlessman, J.L. (2014) The 2\/2 Hemoglobin from the Cyanobacterium <em>Synechococcus<\/em> sp. PCC 7002 with Covalently Attached Heme: Comparison of X-ray and NMR structures. <em>Proteins<\/em> <strong>82<\/strong>:528\u2013534. <a href=\"http:\/\/dx.doi.org\/10.1002\/prot.24409\">doi:10.1002\/prot.24409<\/a><\/li>\n<li>Johnson, E.A. and Lecomte, J.T.J. The Globins of Cyanobacteria and Algae. <em>Advances in Microbial Physiology<\/em> <strong>63<\/strong>:195\u2013272. <a href=\"http:\/\/dx.doi.org\/10.1016\/B978-0-12-407693-8.00006-6\">doi:10.1016\/B978-0-12-407693-8.00006-6<\/a><\/li>\n<li>Preimesberger, M.R., Wenke, B.B., Gilevicius, L., Pond, M.P., and Lecomte, J.T.J. (2013) Covalent Heme Attachment in <em>Synechocystis<\/em> Hemoglobin: Implications for Facile Histidine Posttranslational Modification. <em>Biochemistry<\/em> <strong>52<\/strong>:3478\u20133488. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi400289e\">doi:10.1021\/bi400289e<\/a><\/li>\n<\/ul>\n<ul>\n<li>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. <em>Biochimica et Biophysica Acta<\/em> <strong>1834<\/strong>:1910\u20131922. <a href=\"http:\/\/dx.doi.org\/10.1016\/j.bbapap.2013.04.016\">doi:10.1016\/j.bbapap.2013.04.016<\/a><\/li>\n<li>Lecomte, J.T.J. and Falzone, C.J. (2013) Protein Structure: Unusual Covalent Bonds. <em>Nature Encyclopedia of Life Sciences<\/em>. <a href=\"http:\/\/dx.doi.org\/10.1002\/9780470015902.a0003015.pub2\">doi:10.1002\/9780470015902.a0003015.pub2<\/a><\/li>\n<li>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. <em>Biochemistry<\/em> <strong>51<\/strong>:5733\u20135747. <a href=\"http:\/\/dx.doi.org\/%2010.1021\/bi300624a\">doi:10.1021\/bi300624a<\/a><\/li>\n<li>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 <sup>19<\/sup>F NMR Study of <em>Synechococcus<\/em> sp. PCC 7002 GlbN. <em>Chemistry and Biodiversity<\/em> <strong>9<\/strong>:1703\u20131717. <a href=\"http:\/\/dx.doi.org\/10.1002\/cbdv.201100448\">doi:10.1002\/cbdv.201100448<\/a><\/li>\n<li>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<em> Synechocystis<\/em> sp. PCC 6803 and<em> Synechococcus<\/em> sp. PCC 7002. <em>Journal of Bioinorganic Chemistry<\/em> <strong>17<\/strong>:599-609. <a href=\"http:\/\/dx.doi.org\/10.1007\/s00775-012-0880-5\">doi:10.1007\/s00775-012-0880-5<\/a><\/li>\n<li>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 <em>Helicobacter hepaticus<\/em>. <em>IUBMB Life<\/em> <strong>63<\/strong>:197\u2013205 <a href=\"http:\/\/dx.doi.org\/10.1002\/iub.430\">doi:10.1002\/iub.430<\/a><\/li>\n<li>Nothnagel, H.J., Preimesberger, M.R., Pond, M.P., Winer, B.Y., Adney, E.A., and Lecomte, J.T.J. (2011) Chemical Reactivity of <em>Synechococcus<\/em> sp. PCC 7002 and <em>Synechocystis<\/em> sp. PCC 6803 Hemoglobins: Covalent Heme Attachment and Bishistidine Coordination. <em>Journal of Biological Inorganic Chemistry<\/em> <strong>16<\/strong>:539\u2013552. <a href=\"http:\/\/dx.doi.org\/10.1007\/s00775-011-0754-2\">doi:10.1007\/s00775-011-0754-2<\/a><\/li>\n<li>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 <em>Synechococcus<\/em> sp. PCC 7002. <em>Biochemistry<\/em> <strong>49<\/strong>:7000\u20137011. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi100463d\">doi:10.1021\/bi100463d<\/a><\/li>\n<li>Pond, M.P., Vuletich, D.A., Falzone, C.J., Majumdar, A., and Lecomte, J.T.J. (2009) <sup>1<\/sup>H, <sup>15<\/sup>N, and <sup>13<\/sup>C Resonance Assignments of the 2\/2 Hemoglobin from the Cyanobacterium <em>Synechococcus<\/em> sp. PCC 7002 in the Ferric Bis-histidine State. <em>Biomolecular NMR Assignments<\/em> <strong>3<\/strong>:211\u2013214. <a href=\"http:\/\/dx.doi.org\/10.1007\/s12104-009-9177-1\">doi:10.1007\/s12104-009-9177-1<\/a><\/li>\n<li>Nothnagel, H.J., Love, N., and Lecomte, J.T.J. (2009) The Role of the Heme Distal Ligand in the Post-translational Modification of <em>Synechocystis<\/em> Hemoglobin. <em>Journal of Bioinorganic Chemistry<\/em> <strong>103<\/strong>:107\u2013116. <a href=\"http:\/\/dx.doi.org\/10.1016\/j.jinorgbio.2008.09.009\">doi:10.1016\/j.jinorgbio.2008.09.009<\/a><\/li>\n<\/ul>\n<ul>\n<li>Graham, J.E., Lecomte, J.T.J., and Bryant, D.A. (2008) Synechoxanthin: an Aromatic C40 Xanthophyll is a Major Carotenoid in the Cyanobacterium <em>Synechococcus<\/em> sp. PCC 7002. <em>Journal of Natural Products<\/em> <strong>71<\/strong>:1647\u20131650. <a href=\"http:\/\/dx.doi.org\/10.1021\/np800310b\">doi:10.1021\/np800310b<\/a><\/li>\n<li>Davis, R.B. Jr. and Lecomte, J.T.J. (2008) Structural Propensities in the Heme Binding Region of Apocytochrome <em>b<\/em><sub>5<\/sub>. II. Heme Conjugates. <em>Biopolymers\u2013Peptide Science<\/em> <strong>90<\/strong>:556\u2013566. <a href=\"http:\/\/dx.doi.org\/10.1002\/bip.20995\">doi:10.1002\/bip.20995<\/a><\/li>\n<li>Davis, R.B. Jr. and Lecomte, J.T.J. (2008) Structural Propensities in the Heme Binding Region of Apocytochrome <em>b<\/em><sub>5<\/sub>. I. Free Peptides. <em>Biopolymers\u2013Peptide Science<\/em> <strong>90<\/strong>:544\u2013555. <a href=\"http:\/\/dx.doi.org\/10.1002\/bip.20996\">doi:10.1002\/bip.20996<\/a><\/li>\n<li>Lecomte, J.T.J., Mukhopadhyay, K., and Pond, M.P. (2008) Structural and Thermodynamic Encoding in the Sequence of Rat Microsomal Cytochrome <em>b<\/em><sub>5<\/sub>. <em>Biopolymers<\/em> <strong>89<\/strong>:428\u2013442. <a href=\"http:\/\/dx.doi.org\/10.1002\/bip.20892\">doi:10.1002\/bip.20892<\/a><\/li>\n<li>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. <em>Gene<\/em> <strong>398<\/strong>:12\u201328. <a href=\"http:\/\/dx.doi.org\/10.1016\/j.gene.2007.02.046\">doi:10.1016\/j.gene.2007.02.046<\/a><\/li>\n<li>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. <em>Protein Science<\/em> <strong>16<\/strong>:863\u2013879. <a href=\"http:\/\/dx.doi.org\/10.1110\/ps.062469507\">doi:10.1110\/ps.062469507<\/a><\/li>\n<li>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 <em>Synechococcus<\/em> sp. PCC 7002 Hemoglobin. <em>Biochemistry<\/em> <strong>45<\/strong>:14075\u201314084. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi061532g\">doi:10.1021\/bi061532g<\/a><\/li>\n<li>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 <em>Synechocystis<\/em> sp. PCC 6803 Hemoglobin. <em>Biochemistry<\/em> <strong>45<\/strong>:11401\u201311413. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi060691x\">doi:10.1021\/bi060691x<\/a><\/li>\n<li>Davis Jr, R.B., and Lecomte, J.T.J. (2006) A Dynamic N-cap Motif in Cytochrome <em>b<\/em><sub>5<\/sub>. Evidence for a pH-controlled Conformational Switch. <em>Proteins: Structure, Function, and Bioinformatics<\/em>\u00a0 <strong>63<\/strong>:336\u2013348. <a href=\"http:\/\/dx.doi.org\/10.1002\/prot.20759\">doi:10.1002\/prot.20759<\/a><\/li>\n<li>Vuletich, D.A., and Lecomte, J.T.J. (2006) A Phylogenetic and Structural Analysis of Truncated Hemoglobins. <em>Journal of Molecular Evolution<\/em> <strong>62<\/strong>:196\u2013210. <a href=\"http:\/\/dx.doi.org\/10.1007\/s00239-005-0077-4\">doi:10.1007\/s00239-005-0077-4<\/a><\/li>\n<\/ul>\n<ul>\n<li>Lecomte, J.T.J., Vuletich, D.A, and Lesk, A. M. (2005) Structural Divergence and Distant Relationships in Proteins: Evolution of the Globin Family. <em>Current Opinion in Structural Biology<\/em> <strong>15<\/strong>:290\u2013301. <a href=\"http:\/\/dx.doi.org\/10.1016\/j.sbi.2005.05.008\">doi:10.1016\/j.sbi.2005.05.008<\/a><\/li>\n<li>Lecomte, J.T.J., Vu, B.C., and Falzone,C.J. (2005) Structural and Dynamic Properties of <em>Synechocystis<\/em> sp. PCC 6803 Hb Revealed by Reconstitution with Zn-Protoporphyrin IX. <em>Journal of Inorganic Biochemistry<\/em> <strong>99<\/strong>:1585\u20131592. <a href=\"http:\/\/dx.doi.org\/10.1016\/j.jinorgbio.2005.04.018\">doi:10.1016\/j.jinorgbio.2005.04.018<\/a><\/li>\n<li>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. <em>RNA<\/em> <strong>11<\/strong>:157\u2013172. <a href=\"http:\/\/dx.doi.org\/10.1261\/rna.7177505\">doi:10.1261\/rna.7177505<\/a><\/li>\n<li>Scott, N.L. and Lecomte, J.T.J. (2005) Protein Structure: Unusual Covalent Bonds. <em>Nature Encyclopedia of Life Sciences<\/em> John Wiley &amp; Sons, Ltd: Chichester, UK (updated in 2013)<\/li>\n<li>Knappenberger, J.A., Kraemer-Pecore, C.M., and Lecomte, J.T.J.(2004) Insertion of the Cytochrome <em>b<\/em><sub>5<\/sub> Heme-Binding Loop into an SH3 Domain. Effects on Structure and Stability, and Clues about the Cytochrome\u2019s Architecture. <em>Protein Science<\/em> <strong>13<\/strong>:2899\u20132908. <a href=\"http:\/\/dx.doi.org\/10.1110\/ps.04902704\">doi:10.1110\/ps.04902704<\/a>.<\/li>\n<li>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 <em>Synechocystis<\/em> Hb. <em>Biochemistry<\/em> <strong>43<\/strong>:12622\u201312633. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi048726l\">doi:10.1021\/bi048726l<\/a><\/li>\n<li>Mukhopadhyay, K. and Lecomte, J.T.J. (2004) A Relationship between Heme Binding and Protein Stability in Cytochrome <em>b<\/em><sub>5<\/sub>. <em>Biochemistry<\/em> <strong>43<\/strong>:12227\u201312236. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi0488956\">doi:10.1021\/bi0488956<\/a><\/li>\n<li>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 <em>Synechocystis<\/em> sp. PCC 6803 and <em>Synechococcus<\/em> sp. PCC 7002. <em>Journal of Biological Inorganic Chemistry<\/em> <strong>9<\/strong>:183\u2013194. <a href=\"http:\/\/dx.doi.org\/10.1007\/s00775-003-0512-1\">doi:10.1007\/s00775-003-0512-1<\/a><\/li>\n<li>Kraemer-Pecore, C.M., Lecomte, J.T.J., and Desjarlais, J.R. (2003) A De Novo Redesign of the WW Domain. <em>Protein Science<\/em> <strong>12<\/strong>:2194\u20132205. <a href=\"http:\/\/dx.doi.org\/10.1110\/ps.03190903\">doi:10.1110\/ps.03190903<\/a><\/li>\n<\/ul>\n<ul>\n<li>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 <em>Synechocystis<\/em> sp. PCC 6803 in its Hemichrome State. <em>Journal of Molecular Biology<\/em> <strong>324<\/strong>:1015\u20131029.<a href=\"http:\/\/dx.doi.org\/10.1016\/s0022-2836(02)01093-8\"> doi:10.1016\/s0022-2836(02)01093-8<\/a><\/li>\n<li>Vu, B.C., Jones, A.D., and Lecomte, J.T.J. (2002) Novel Histidine-Heme Covalent Linkage in a Hemoglobin. <em>Journal of the American Chemical Society<\/em> <strong>124<\/strong>:8544\u20138545. doi:10.1021\/ja026569<\/li>\n<li>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 <em>Synechococcus<\/em> sp. PCC 7002: Evidence for Hexacoordination and Covalent Adduct Formation in the Ferric Recombinant Protein. <em>Biochemistry<\/em> <strong>22<\/strong>:6902\u20136910. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi025609m\">doi:10.1021\/bi025609m<\/a><\/li>\n<li>Falzone, C.J. and Lecomte, J.T.J. (2002) Letter to the Editor: Assignment of the <sup>1<\/sup>H, <sup>13<\/sup>C, and <sup>15<\/sup>N Signals of <em>Synechocystis<\/em> sp. PCC 6803 Methemoglobin. <em>Journal of Biomolecular NMR<\/em> <strong>23<\/strong>:71\u201372.<\/li>\n<li>Lee, K.K., Fitch, C.A., Lecomte, J.T.J., and Garc\u00eda-Moreno E, B. (2002) Electrostatic Effects in Highly Charged Proteins: Salt Sensitivity of pKa Values of Histidines in Staphylococcal Nuclease. <em>Biochemistry<\/em> <strong>41<\/strong>:5656\u20135667. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi0119417\">doi:10.1021\/bi0119417<\/a><\/li>\n<li>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 <em>Synechocystis<\/em> sp. PCC 6803. <em>Biochemistry<\/em> <strong>40<\/strong>:6541\u20136552. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi010226u\">doi:10.1021\/bi010226u<\/a><\/li>\n<li>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 <em>b<\/em><sub>5<\/sub>. <em>Biochemistry<\/em> <strong>40<\/strong>:4879\u20134891. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi002681g\">doi:10.1021\/bi002681g<\/a><\/li>\n<li>Kao, Y.H., Fitch, C.A., Bhattacharya, S., Sarkisian, C.J., Lecomte, J.T.J., and Garc\u00eda-Moreno E., B. (2000) Salt Effects on Ionization Equilibria of Histidines in Myoglobin. <em>Biophysical Journal<\/em> <strong>79<\/strong>:1637\u20131654.<\/li>\n<li>Scott, N.L and Lecomte, J.T.J. (2000) Cloning, Expression, Purification, and Preliminary Characterization of a Putative Hemoglobin from the Cyanobacterium <em>Synechocystis<\/em> sp. PCC 6803. <em>Protein Science<\/em> <strong>9<\/strong>:587\u2013597.<\/li>\n<\/ul>\n<ul>\n<li>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 <em>Nostoc<\/em> sp. Strain PCC 8009. <em>Biochemistry<\/em> <strong>38<\/strong>:13736\u201313746. <a href=\"http:\/\/doi:10.1021\/bi9910373\">doi:10.1021\/bi9910373<\/a><\/li>\n<li>Lecomte, J.T.J., Sukits, S.F., Bhattacharya, S., and Falzone, C.J. (1999) Conformational Properties of Native Sperm Whale Apomyoglobin in Solution. <em>Protein Science<\/em> <strong>8<\/strong>:1484\u20131491.<\/li>\n<li>Bhattacharya, S., Falzone, C.J., and Lecomte, J.T.J. (1999) The Backbone Dynamics of Apocytochrome <em>b<\/em><sub>5<\/sub> in Its Native, Partially Folded State. <em>Biochemistry<\/em> <strong>38<\/strong>:2577\u20132589. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi995081u\">doi:10.1021\/bi995081u<\/a><\/li>\n<li>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 <em>b<\/em><sub>5<\/sub>. <em>Protein Science<\/em> <strong>7<\/strong>:1983\u20131993.<\/li>\n<li>Bhattacharya, S. and Lecomte, J.T.J. (1997) The Temperature Dependence of Histidine Ionization Constants in Myoglobin. <em>Biophysical Journal<\/em> <strong>73<\/strong>:3241\u20133256.<\/li>\n<li>Bhattacharya, S., Sukits, S.F., MacLaughlin, K.L, and Lecomte, J.T.J. (1997) The Tautomeric State of Histidines in Myoglobin. <em>Biophysical Journal<\/em> <strong>73<\/strong>:3230\u20133240.<\/li>\n<li>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 <em>b<\/em><sub>5<\/sub>. <em>Biochemistry<\/em> <strong>35<\/strong>:6519\u20136526. <a href=\"http:\/\/dx.doi.org\/10.1021\/bi960501q\">doi:10.1021\/bi960501q<\/a><\/li>\n<li>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. <em>Proteins: Structure Function and Genetics<\/em> <strong>25<\/strong>:267\u2013285.<\/li>\n<li>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 <em>Synechococcus<\/em> sp. Strain PCC 7002: a Photosystem I Protein that Shows Structural Homology with SH3 Domains. <em>Biochemistry<\/em> <strong>33<\/strong>:6052\u20136062.<\/li>\n<li>Falzone, C.J., Kao, Y.-H., Zhao, J., MacLaughlin, K.L., Bryant, D.A., and Lecomte, J.T.J. (1994) <sup>1<\/sup>H and <sup>15<\/sup>N NMR Assignments of PsaE, a Photosystem I Subunit from the Cyanobacterium <em>Synechococcus<\/em> sp. Strain PCC 7002. <em>Biochemistry<\/em> <strong>33<\/strong>:6043\u20136051.<\/li>\n<li>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. <em>Protein Science<\/em> <strong>3<\/strong>:267\u2013281.<\/li>\n<li>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. <em>Journal of the American Chemical Society<\/em> <strong>115<\/strong>:9754\u20139762.<\/li>\n<\/ul>\n<ul>\n<li>Moore, C.D. and Lecomte, J.T.J. (1993) Characterization of an Independent Structural Unit in Apocytochrome <em>b<\/em><sub>5<\/sub>. <em>Biochemistry<\/em> <strong>32<\/strong>:199\u2013207.<\/li>\n<li>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. <em>Journal of the American Chemical Society<\/em> <strong>114<\/strong>:11000\u201311001.<\/li>\n<li>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. <em>Biochemistry<\/em> <strong>31<\/strong>:6481\u20136491.<\/li>\n<li>Falzone, C.J., Benesi, A.J., and Lecomte, J.T.J. (1992) Characterization of Taxol in Methylene Chloride by NMR Spectroscopy. <em>Tetrahedron Letters<\/em> <strong>33<\/strong>:1169\u20131172.<\/li>\n<li>Lecomte, J.T.J. and Moore, C.D. (1991) Helix Formation in Apocytochrome <em>b<\/em><sub>5<\/sub>: The Role of a Neutral Histidine at the N-Cap Position. <em>Journal of the American Chemical Society<\/em> <strong>113<\/strong>:9663\u20139665.<\/li>\n<li>Moore, C.D., Al-Misky, O.N., and Lecomte, J.T.J. (1991) Similarities in Structure between Holocytochrome <em>b<\/em>5 and Apocytochrome <em>b<\/em>5: NMR Studies of the Histidine Residues. <em>Biochemistry<\/em> <strong>30<\/strong>:8357\u20138365.<\/li>\n<li>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. <em>Journal of Magnetic Resonance<\/em> <strong>94<\/strong>:112\u2013122.<\/li>\n<li>Cocco, M.J. and Lecomte, J.T.J. (1990) Characterization of Hydrophobic Cores in Apomyoglobin: A Proton NMR Spectroscopy Study. <em>Biochemistry<\/em> <strong>29<\/strong>:11067\u201311072.<\/li>\n<li>Lecomte, J.T.J. and Cocco, M.J. (1990) Structural Features of the Protoporphyrin-Apomyoglobin Complex: A Proton NMR Spectroscopy Study. <em>Biochemistry<\/em> <strong>29<\/strong>:11057\u201311067.<\/li>\n<li>Moore, C.D. and Lecomte, J.T.J. (1990) Structural Properties of Apocytochrome <em>b<\/em><sub>5<\/sub>: Presence of a Stable Native Core. <em>Biochemistry<\/em> <strong>29<\/strong>:1984\u20131989.<\/li>\n<\/ul>\n<ul>\n<li>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. <em>Journal of Molecular Biology<\/em> <strong>209<\/strong>:235\u2013246.<\/li>\n<li>Emerson, S.D., Lecomte, J.T.J., and La Mar, G.N. (1989) <sup>1<\/sup>H NMR Resonance Assignment and Dynamic Analysis of Phenylalanine CD1 in Low-Spin Ferric Complex of Sperm Whale Myoglobin. <em>Journal of the American Chemical Society<\/em> <strong>110<\/strong>:4176\u20134182.<\/li>\n<li>Lecomte, J.T.J. and La Mar, G.N. (1987) <sup>1<\/sup>H NMR Probe for Hydrogen Bonding of Distal Residues to Bound Ligands in Heme Proteins: Isotope Effect on Heme Electronic Structure of Myoglobin. <em>Journal of the American Chemical Society<\/em> <strong>109<\/strong>:7219\u20137220.<\/li>\n<li>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. <em>Journal of Molecular Biology<\/em> <strong>197<\/strong>:101\u2013110.<\/li>\n<li>Lecomte, J.T.J., Kaplan, D., Llin\u00e1s, M., Thunberg, E., and Samuelsson, G. (1987) Proton Magnetic Resonance Characterization of Phoratoxins and Homologous Proteins Related to Crambin. Biochemistry <strong>26<\/strong>:1187\u20131194.<\/li>\n<li>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 &#8220;Sulfhemin&#8221;: Participation of the 4-Vinyl Group in the Saturation of the Pyrrole in One of the Forms of Sulfmyoglobin. <em>Journal of the American Chemical Society<\/em> <strong>108<\/strong>:7108\u20137110.<\/li>\n<li>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. <em>Biochemistry<\/em> <strong>25<\/strong>:5863\u20135646.<\/li>\n<li>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 <strong>108<\/strong>:5568\u20135573.<\/li>\n<li>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. <em>Biochemical and Biophysical Research Communications<\/em> <strong>135<\/strong>:309\u2013315.<\/li>\n<li>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. <em>European Biophysics Journal<\/em> <strong>13<\/strong>:373\u2013381.<\/li>\n<\/ul>\n<ul>\n<li>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. <em>Biochemistry<\/em> <strong>24<\/strong>:7388\u20137395.<\/li>\n<li>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 <strong>64<\/strong>:521\u2013526.<\/li>\n<li>Lecomte, J.T.J., Johnson, R.D., and La Mar, G.N. (1985) Characterization of Heme Orientational Disorder in Myoglobin by Nuclear Overhauser Effect. <em>Biochimica et Biophysica Acta<\/em> <strong>829<\/strong>:268\u2013274.<\/li>\n<li>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 (<em>Dicroc\u0153lium dendriticum<\/em>) Methemoglobin. <em>Journal of Molecular Biology<\/em> <strong>180<\/strong>:357\u2013370.<\/li>\n<li>Lecomte, J.T.J. and Llin\u00e1s, M. (1984) Characterization of the Aromatic Proton Magnetic Resonance Spectrum of Crambin. <em>Biochemistry<\/em> <strong>23<\/strong>:4799\u20134807.<\/li>\n<li>Lecomte, J.T.J. and Llin\u00e1s, M. (1984) Spectral Patterns of Rapidly Flipping Tyrosyl Rings, a Study of Crambin in Organic Solvents. <em>Journal of the American Chemical Society<\/em> <strong>106<\/strong>:2741\u20132748.<\/li>\n<li>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. <em>Photochemistry and Photobiology<\/em> <strong>39<\/strong>:213\u2013219.<\/li>\n<li>Lecomte, J.T.J., Jones, B.L., and Llin\u00e1s, M. (1982) Proton Magnetic Resonance Studies of Barley and Wheat Thionins: Structural Homology with Crambin. <em>Biochemistry<\/em> <strong>21<\/strong>:4843\u20134849.<\/li>\n<li>Lecomte, J.T.J., De Marco, A., and Llin\u00e1s, M. (1982) Analysis of the Methyl Proton NMR Spectrum of Crambin, a Hydrophobic Protein. Biochimica et Biophysica Acta <strong>703<\/strong>:223\u2013230.<\/li>\n<li>De Marco, A., Lecomte, J.T.J., and Llin\u00e1s, M. (1981) Solvent and Temperature Effects on Crambin, a Hydrophobic Protein, as Investigated by Proton Magnetic Resonance. <em>European Journal of Biochemistry<\/em> <strong>119<\/strong>:483\u2013490.<\/li>\n<\/ul>\n<ul>\n<li>Llin\u00e1s, M. and Lecomte, J.T.J. (1980) Solvent and Temperature Effects on Crambin, a Hydrophobic Protein. <em>Biophysical Journal<\/em> <strong>32<\/strong>:90\u201391.<\/li>\n<li>Llin\u00e1s, M., De Marco, A., and Lecomte, J.T.J. (1980) Proton Magnetic Resonance of Crambin, a Hyperstable Hydrophobic Protein, at 250 and 600 MHz. <em>Biochemistry<\/em> <strong>19<\/strong>:1140\u20131145.<\/li>\n<li>Piette, J.-L., Lecomte, J.T.J., and Lecomte, J. (1978) Propri\u00e9t\u00e9s Convulsivantes de Quelques D\u00e9riv\u00e9s Organo-S\u00e9l\u00e9ni\u00e9s. <em>Comptes Rendus des S\u00e9ances de la Soci\u00e9t\u00e9 de Biologie<\/em> <strong>172<\/strong>:383\u2013387.<\/li>\n<li>Piette, J.-L., Lecomte, J.T.J., Damas, J., and Lecomte, J. (1977) Toxicit\u00e9 Compar\u00e9e des Acides M\u00e9thylthio, M\u00e9thyls\u00e9l\u00e9no, Ac\u00e9tyl-2-Benzo\u00efque chez le Rat. <em>Bulletin de la Soci\u00e9t\u00e9 Royale des Sciences de Li\u00e8ge<\/em> <strong>11-12<\/strong>:433\u2013439.<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>Selected Publications (MyBib Listing) Martinez Grundman, J.E., Schultz, T.D., Schlessman, J.L., Johnson, E. A., Gillilan, R.E., and Lecomte, J.T.J. (2025) Extremophilic Hemoglobins: The Structure of Shewanella benthica Truncated Hemoglobin N.\u00a0 Journal of Biological Chemistry,\u00a0301:108223.\u00a0 doi:10.1016\/j.jbc.2025.108223 Martinez Grundman, J.E., Schultz, T.D., Schlessman, J.L., Liu, K., Johnson, E.A., and Lecomte, J.T.J.\u00a0 (2024) Heme d Formation in a [&hellip;]<\/p>\n","protected":false},"author":40,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"open","ping_status":"open","template":"","meta":{"_acf_changed":false,"footnotes":""},"class_list":["post-7","page","type-page","status-publish","hentry"],"acf":[],"_links":{"self":[{"href":"https:\/\/sites.krieger.jhu.edu\/lecomte-lab\/wp-json\/wp\/v2\/pages\/7","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/sites.krieger.jhu.edu\/lecomte-lab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.krieger.jhu.edu\/lecomte-lab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.krieger.jhu.edu\/lecomte-lab\/wp-json\/wp\/v2\/users\/40"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.krieger.jhu.edu\/lecomte-lab\/wp-json\/wp\/v2\/comments?post=7"}],"version-history":[{"count":4,"href":"https:\/\/sites.krieger.jhu.edu\/lecomte-lab\/wp-json\/wp\/v2\/pages\/7\/revisions"}],"predecessor-version":[{"id":209,"href":"https:\/\/sites.krieger.jhu.edu\/lecomte-lab\/wp-json\/wp\/v2\/pages\/7\/revisions\/209"}],"wp:attachment":[{"href":"https:\/\/sites.krieger.jhu.edu\/lecomte-lab\/wp-json\/wp\/v2\/media?parent=7"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}