J P Emerson Research Group
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ABOUT
Transition metals are elemental to survival!
     Welcome to the Emerson Research Group. We are a diverse group of scientists interested in studying novel reactions. Most of the chemical and biochemical systems under investigation in the ERG are focused on the chemistry of first-row transition metal ions, where their ligand archtecture plays a key role in controlling their chemistry.  To study these systems we use tools from biology, biochemistry, biophysics (especially calorimetry), organic chemistry, and inorganic chemistry. A couple of our current projects are shown to the right. If you are interested in collaborating with us or joining our team, please feel free to contact me! 

- Joe Emerson
CURRENT PROJECTS

· Substrate and cofactor cooperativity in air-sensitive, nonheme iron(II) proteins

· Conformational stability changes in proteins induced by metal ion(s) coordination

· Metal ion transcription factors from S. pneumoniae

· N- and C- atom transfer reactions catalyzed by hybrid and classical catalytic systems.


Joseph P. Emerson, Ph.D.
Associate Professor
Department of Chemistry
Mississippi State University

jemerson at chemistry.msstate.edu

662.325.4633


Metalloprotein Biochemistry /Biophysics/Bioinorganic Chemistry
Nearly half of all proteins contain some sort of metal ion binding site. These metal ions play different roles in biology, where some offer increased stability of maromolecule struture while others are the focial point of reactivity. The Emerson lab is interested in the fundamental roles metal ions play in stabilizing proteins and DNA, and how these  ions augment their local environment to facilitate biological and bio-inspired transformations. 

Inorganic Chemistry/Catalysis
First row transition metals are highly abundent and offer a wide-range of catalytic capabilities. The Emerson lab is interested in developing bio-inspired catalytic systems for asymmetric transformations. 
MEMBERS
Graduate students
Daniel K Wolgemuth
Danny joined the group in 2016 after completing his BS degree at Mississippi State. Danny's research project is aimed at designing new sustanable catalytic systems and using template biomolecules to impact catalyst selectivity.

dkw86 at msstate.edu

Sydnee D Elmore
Sydnee joined the group in 2017 after completing her BS degree at Mississippi State. Sydnee's project is aimed at using MnTmPyP4 based catalysts for asymmetric N-atom transfer chemistry.

sde59 at msstate.edu
Kayla D McConnell
Kayla joined the group as a PhD student in 2015 after completing an MS degree at TWU where she worked with Dick Sheardy. She is currently studying the biophysics of transition metal ion binding to proteins and other biomolecules.

kdm597 at msstate.edu
Zhenyu "Tony" Zhu
Tony joined the ERG in the fall of 2017. Tony's research project is aimed at using bio-inspired catalysts and metalloproteins for novel transformations. 

zz224 at msstate.edu
ASM Saem
Saem joined the ERG in the fall of 2017. Originally from Bangladesh, Saem's projects are aimed at the zinc(II) dependent transcription factor AdcR and its interactions with DNA.

as4767 at msstate.edu
James D Cope
James joined the group in 2018. James' projects are aimed at developing new hybrid catalyst systems for asymmetric transformations.

jdc1032 at msstate.edu
Prakash Khanal
Prakash joined the ERG in the summer of 2018. Prakash's project is focused on a copper(II) dependent transcription factor in S. pneumoniae

pk510 at msstate.edu


New graduate students!
The Emerson Research Group is always looking for new members. Students interested in joining our group can start by applying to the chemistry gradute program at Mississippi State University. You can explore our program at the following link:

 Apply now!


Undergraduate students
Wes Harrison
Wes (BS CHE, 2019) joined the ERG in 2018 as an undergraduate researcher. Wes has worked on a number of projects including some focused on sustainable catalysis using water soluble heme complexes. 
Josh Porter
Josh (BS BCH, 2019) joined the group in 2016. Josh's project is aimed at measuring the thermodynamic properties of metal ion binding to carbonic anhydrase II. Josh has also worked with Dr. Nate DeYonker at the University of Memphis on theoritical aspects of this product.
Zoe Fokakis
Zoe (BS CH, 2020) joined the ERG in January 2018, where she is working to over-express and isolate several proteins for further characterization. 
Margaret Lee
Margaret (BS BCH, 2020+) joined the ERG in January 2018, where she is working to over-express and isolate several metalloproteins for further characterization. 
Raychele Bowling
Raychele (BS BCH, 2020+) joined the ERG in January 2018, where she is working to over-express and isolate several metalloproteins for further characterization. 
Becky Woodruff
Bechy (BS BCH, 2020+) joined the ERG in January 2018, where she is working to over-express and isolate several metalloproteins for further characterization. 
Dylan Russell
Dylan (BS CHE, 2019) joined the group in August of 2017. His project is aimed at building new cyclopropanation reactions using copper(II) catalysts in traditional and sustaninable solvent systems.

Nathan Allgaier
Nathan (BS CH, 2020) joined the ERG in August 2017. Nathan is working to over-express and isolate human carbonic anhydrase II for a range of biophysical studies. 
Jacob Nichols
Jacob (BS CH, 2020) joined the group in January 2018, where his projects are aimed at isolating two flavin-dependent enzymes in the pyrrolnitrin biosynthetic pathway. 
NEWS
The SRBC is heading to Louisiana in 2019!
The 12th annual meeting of the Southeast Regional Biophyscial Consortium (formerally known as the Mississippi Regional Biophysical Consortium) is being hosted at LSU (Baton Rouge, LA) in May of 2019. More information will be available soon!
Mingjie Li and Henry Valle graduate from the ERG!
Mingjie Li (PhD CH, 2018) and Henry Valle (PhD CH, 2018) participated in the December graduation cermimony at MSU. Congrats Mingjie and Henry!
       Josh Porter to Med School!
Josh Porter (BS Biochem, 2016-2019) was recently accepted in to the MD program at the University of Tennessee Health Science Center in Memphis, TN. Congrats Josh!
PUBLICATIONS

32. 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. [link]

31. 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 [link] 

30. 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 [link] 

29. 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 [link] 

28. 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; 1851:987-994. doi:10.1016/j.bbagen.2017.02.018 [link] 

27. 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 [link]

26. 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.[link
 
25. 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 [link
 
24. 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 [link
 
23. 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 [link]  
 
22. 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 [link]  
 
21. 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 [link]  
 
20. Calorimetry  
      Joseph P. Emerson, Vu H. Le, Edwin A. Lewis  
      eLS (Encyclopedia of Life Sciences), 2012  
      John Wiley & Sons Ltd, http://www.els.net [link]  
 
19. 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 [link]  
 
18. 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 [link]  
 
17. 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 [link]  
 
16. 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 [link]  
 
15. 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 [link]  
 
14. 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 [link]  
 
13. 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 [link]  
 
12. 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 [link]  
 
11. 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 [link]  
     
     “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
 
10. Post-translational Self-hydroxylation 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 [link]  
 
 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 [link]  
 
 8. 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 [link]  
 
 7. 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
 
 6. 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 [link]  
 
 5. 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 [link]  
 
 4. 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 [link]  
 
 3. 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 [link]  
 
 2. 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 [link]  
 
 1. 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 [link]