Earlier work from the ESRG
Streptococcus pneumoniae metal homeostasis alters cellular metabolism.
Lindsey R. Burcham, Rebecca A. Hill, Rachel C. Caulkins, Joseph P. Emerson, Bindu Nanduri, Jason W. Rosch, Nicholas C. Fitzkee, Justin A. Thornton, Metallomics, 2020, 12, 1416-1427. doi: 10.1039/D0MT00118J
Tuning the Copper(II)/Copper(I) Redox Potential for More Robust Copper-Catalyzed C–N Bond Forming Reaction.
James D. Cope, Henry U. Valle, Ruby S. Hall, Ekta Goel, S. Biswas, Michael P. Hendrich, David O. Wipf, Sean L. Stokes, Joseph P. Emerson, European Journal of Inorganic Chemistry 2020; 2020(14):1278-1285. doi: 10.1002/ejic.201901269.
Thermodynamics of iron(II) and substrate binding to the ethylene-forming enzyme.
Mingjie Li, Salette Martinez, Robert P. Hausinger, Joseph P. Emerson, Biochemistry 2018; 57:5696-5705. doi: 10.1021/acs.biochem.8b00730.
Synthesis, Characterization, and Structure of a [(phen)2Cu(OTf)]OTf Complex; An Efficient Nitrogen Transfer Pre-catalyst.
Henry U. Valle, Kathleen M. Riley, Dylan E. Russell, Daniel K. Wolgemuth, Shanterell L. Redd, Sean L. Stokes, Joseph P.
Emerson, ChemistrySelect 2018; 22:1123-1135. doi: 10.1002/slct.201800588
The Irving William series and the 2-His-1-carboxylate facial triad: A thermodynamic study of Mn2+, Fe2+, and Co2+ binding to taurine/α-ketoglutarate dioxygenase (TauD).
Mingjie Li, Kate L. Henderson, Salette Martinez, Robert P. Hausinger, Joseph P. Emerson, Journal of Biological Inorganic
Chemistry, 2018; doi: 10.1007/s00775-018-1574-4.
Resolving Distinct Molecular Origins for Copper Effects on PAI-1
Joel C. Bucci, Carlee S. McClintock, Yuzhuo Chu, Gregory L. Ware, Kayla D. McConnell, Joseph P. Emerson, Cynthia B.
Peterson, Journal of Biological Inorganic Chemistry, 2017; 22:1123-1135. doi:10.1007/s00775-017-1489-5
Global Stability of an α-Ketoglutarate-Dependent Dioxygenase (TauD) Using Differential Scanning Calorimetry
Kate L. Henderson, Mingjie Li, Salette Martinez, Robert P. Hausinger, Joseph P. Emerson, Biochimica Biophysica Acta 2017; 1851-994. doi: 10.1016/j.bbagen.2017.02.018
ITC Methods for Assessing Buffer/Protein Interactions using Steady-State Kinetics: A reactivity study of Homoprotocatechuate 2,3-Dioxygenase
Kate L. Henderson, Delta K. Boyles, Vu H. Le, Edwin A. Lewis, and Joseph P. Emerson, Methods in Enzymology 2016; 567; 257-78. doi: 10.1016/bs.mie.2015.08.034
Calorimetric and spectroscopic investigations of the binding of metallated porphyrins to G-quadruplex DNA
Jesse I. DuPont, Kate L. Henderson, Amanda Metz, Vu H. Le, Joseph P. Emerson, Edwin A. Lewis, Biochimica Biophysica Acta 2015 1860(5):902-9. doi: 10.1016/j.bbagen.2015.09.004.
Thermodynamics of Substrate Binding to the Metal Site in Homoprotocatechuate 2,3-Dioxygenase: Using ITC under anaerobic conditions to study enzyme-substrate interactions
Kate L. Henderson, Danielle H. Francis, Edwin A. Lewis, Joseph P. Emerson, Biochimica Biophysica Acta, 2015 1860(5):910-6. doi: 10.1016/j.bbagen.2015.07.013
Characterization of the Copper(II) Binding Sites in Human Carbonic Anhydrase II.
Whitnee L. Nettles, He Song, Nicholas C. Fitzkee, Joseph P. Emerson, Inorganic Chemistry, 2015 54(12), 2278-2283. DOI: 10.1021/acs.inorgchem.5b00057
Iodide-Induced Organothiol Desorption and Photochemical Reaction, Gold Nanoparticle (AuNP) Fusion, and SERS Signal
Reduction in Organothiol-Containing AuNP Aggregates
Ganganath S. Perera, Allen LaCour, Yadong Zhou, Kate L. Henderson, Shengli Zou, Felio Perez, Joseph P. Emerson, Dongmao Zhang, Journal of Physical Chemistry C, 2015 1119(8), 4261-4267. DOI: 10.1021/jp512168z
Calorimetric Assessment of Fe2+ Binding to α-Ketoglutarate/Taurine Dioxygenase: Ironing Out the Energetics of Metal
Coordination by the 2-His-1-Carboxylate Facial Triad
Kate L. Henderson, Tina Müller, Robert Hausinger, Joseph P. Emerson, Inorganic Chemistry, 2015 54(5), 2278-2283. Doi:
10.1021/ic502881q
Building reactive copper centers in human carbonic anhydrase II
He Song, Andrew C. Weirtz, Michael P. Hendrich, Edwin A. Lewis, Joseph P. Emerson, Journal of Biological Inorganic
Chemistry, 2013 18(6), 595-598
Calorimetry
Joseph P. Emerson, Vu H. Le, Edwin A. Lewis, eLS (Encyclopedia of Life Sciences), 2012 John Wiley & Sons Ltd, http://www.els.net
Revisiting Zinc Binding in Human Carbonic Anhydrase
He Song, David L. Wilson, Erik R. Farquhar, Edwin A. Lewis, Joseph P. Emerson, Inorganic Chemistry, 2012 51(20),
11098-105.
Exploring Substrate Binding in Homoprotocatechuate 2,3-Dioxygenase using Isothermal Titration Calorimetry
Kate L. Henderson, Vu H. Le, Edwin A. Lewis, Joseph P. Emerson, Journal of Biological Inorganic Chemistry, 2012 17(7), 991-4.
In vivo Self-Hydroxylation of an Fe-Substituted Manganese Dependent Extradiol Dioxygenase
Erik R. Farquhar, Joseph P. Emerson, Kevin D. Koehntop, Milena Trmcic, Mark Reynolds, Lawrence Que, Jr., Journal of
Biological Inorganic Chemistry, 2011, 16(4), 589-97
Human deoxyhypusine hydroxylase, an enzyme that regulates cell growth, has a nonheme diiron active site that binds O2.
Van V. Vu, Joseph P. Emerson, Marlène Martinho, Yeon S. Kim, Eckard Munck, Myung H. Park, Lawrence Que, Jr.,
Proceedings of the National Academy of Sciences, U.S.A.; 2009, 106(35), 14814-9.
Electron Paramagnetic Resonance Detection of Intermediates in the Enzymatic Cycle of an Extradiol Dioxygenase.
William A. Gunderson, Anna I. Zatsman, Joseph P. Emerson, Erik R. Farquhar, Lawrence Que Jr., John D. Lipscomb, Michael P. Hendrich, Journal of the American Chemical Society; 2008, 130, 14465–7
Synthesis, X-Ray Crystallographic Characterization, and Electronic Structure Studies of a Di-Azide Iron(III) Complex: Implications for the Azide Adducts of Iron(III) Superoxide Dismutase
Laurie E. Grove, Jason K. Hallman, Joseph P. Emerson, Jason A. Halfen, Thomas C. Brunold, Inorganic Chemistry; 2008, 47, 5762-74
Swapping Metals in Fe- and Mn-Dependent Dioxygenases. Evidence for Oxygen Activation Without a Change in Metal Redox State.
Joseph P. Emerson, Elena G. Kovaleva, Erik R. Farquhar, John D. Lipscomb, d Lawrence Que, Jr., Proceedings of the
National Academy of Sciences, U.S.A.; 2008, 105, 7347-52
Reaction of Desulfovibrio vulgaris Two-Iron Superoxide Reductase with Superoxide: Insights from Stopped-flow Spectrophotometry.
Victor W. Huang, Joseph P. Emerson, Donald M. Kurtz, Jr., Biochemistry; 2007, 46, 11342 – 51
Structural “Snap-Shots” along Reaction Pathway of Non-heme Iron Enzymes
Joseph P. Emerson, Erik R. Farquhar, Lawrence Que, Jr., Angewandte Chemie International Edition; 2007, 46; 8553 – 6
“Schnappschüsse” von Strukturen entlang der Reaktionswege von Nicht‐Häm‐Eisenenzymen.
Joseph P. Emerson, Erik R. Farquhar, Lawrence Que, Jr., Angewandte Chemie; 2007, 119 (45), 8705-8708
Post-translational self-hydroxylation: a probe for oxygen activation mechanisms in non-heme iron enzymes
Erik R. Farquhar, Kevin D. Koehntop, Joseph P. Emerson, Lawrence Que, Jr., Biochemical and Biophysical Research
Communications; 2005, 338; 230 – 9
The Role of Histidine 200 in MndD, the Mn(II)-dependent 3,4-Dihydroyphenylacetate 2,3-Dioxygenase from Arthrobacter globiformis CM-2 from Site-Directed Mutagenesis Studies.
Joseph P. Emerson, Michelle L. Wagner, Mark F. Reynolds, Lawrence Que, Jr. Michael J. Sadowsky, Lawrence P. Wackett, Journal of Biological Inorganic Chemistry; 2005, 10; 751-760
The 2-His-1-Carboxylate Facial Triad: A Versatile Platform for Dioxygen Activation at Mononuclear Nonheme Iron(II)
Enzymes.
Kevin D. Koehntop, Joseph P. Emerson, Lawrence Que, Jr., Journal of Biological Inorganic Chemistry; 2005, 10(2); 87-93
Iron Enzymes with Mononuclear Nonheme Active Sites.
Joseph P. Emerson, Mark P. Mehn, Lawrence Que, Jr., Encyclopedia of Inorganic Chemistry II; John Wiley & Sons, Inc.; 2005
Kinetics of the Superoxide Reductase Catalytic Cycle.
Joseph P. Emerson, Eric D. Coulter, Robert S. Phillips, Donald M. Kurtz, Jr., Journal of Biological Chemistry; 2003; 278(41); 39662-8
Spectroscopic Characterization of the [Fe(NHis)4(SCys)] site in 2Fe-Superoxide Reductase for Desulfovibrio vulgaris
Michael D. Clay, Joseph P. Emerson, Eric D. Coulter, Donald M. Kurtz, Jr., Michael K. Johnson, Journal of Biological Inorganic Chemistry, 2003; 8; 671-82
An Engineered Two-Iron Superoxide Reductase Lacking the [Fe(SCys)4] Site Retains its Catalytic Properties in vitro and in vivo.
Joseph P. Emerson, Diane E. Cabelli, Donald M. Kurtz, Jr., Proceedings of the National Academy of Sciences, U.S.A.; 2003; 100, 3802-7
Kinetics and Mechanism of Superoxide Reduction by Two-Iron Superoxide Reductase from Desulfovibrio vulgaris.
Joseph P. Emerson, Eric D. Coulter, Diane E. Cabelli, Robert S. Phillips, Donald M. Kurtz, Jr., Biochemistry; 2002; 41(13); 4348-57
Superoxide Reactivity of Rubredoxin Oxidoreductase (Desulfoferrodoxin) from Desulfovibrio vulgaris: A Pulse Radiolysis
Study.
Eric D. Coulter, Joseph P. Emerson, Donald M. Kurtz, Jr., Diane E. Cabelli, Journal of the American Chemical Society; 2000; 122(46); 11555-6. DOI: 10.1021/ja005583r
Remarkably Efficient Olefin Aziridination Mediated by a New Copper(II) Complex
Jason A Halfen, Jason K. Hallman, John A. Shultz, Joseph P. Emerson, Organometallics; 1999; 18(26); 5435-7. DOI: 10.1021/om9908579