Wayne State University
Timothy Louis Stemmler Ph.D.

Timothy Louis Stemmler Ph.D.

Professor and Director of Research, Pharmaceutical Sciences

Contact

313-577-5712
Timothy.Stemmler@wayne.edu

Office location

EACPHS, Room 3138

Appointments

Professor and Director of Research, Department of Pharmaceutical Sciences

Associate Dean for Postdoctoral Studies

Adjunct Professor, Department of Biochemistry and Molecular Biology

Degrees and Certifications

NIH Postdoctorial Fellow, Department of Biochemistry,
University of Utah, Salt Lake City, UT 2000
Doctor of Philosophy, Biophysical Chemistry, University of Michigan, 1996
Ann Arbor, MI
Masters of Science, Physical Chemistry, St. Louis University, St. Louis, MO 1990
Bachelor of Arts, Physical Chemistry, St. Louis University, St. Louis, MO 1989
 

Awards and Honors

SOM Faculty Research Excellence Award 2011
SOM College Teaching Award2010
Career Development Award2011
Academy of Scholars, Junior Faculty Inductee, WSU 2007
SOM Faculty Research Excellence Award 2006
SOM College Teaching Award2005
Stanford University/SSRL Outstanding Research Highlight 2004
American Heart Assoc. Scientist Development Award 2001-2004
NIH Postdoctoral Fellowship, University of Utah 1996-1999
Outstanding Graduate Student Research Award, Univ. of Michigan 1996
Rackham Conference Travel Award, Univ. of Michigan 1993-1995
Bachelor of Arts in Chemistry, cum Laude, St. Louis University 1989
 

Professional Memberships

REVIEWER – Grants
Czech Science Foundation2013
NIH ZGM1 TRN-A Special Emphasis Study Section (Ad Hoc) 2012-present
NIH ZHD1 Special Emphasis Study Section (Ad Hoc) 2011
NIH ZRG1 Special Emphasis Study Section (Ad Hoc) 2011
Fonds québécois de la recherchesur la nature ET les technologies 2010
Montreal, Canada
NSF – Biomolecules Study Section (Ad Hoc) 2009-present
NIH – P41 SSRL Facility Grant Study Section (Full Member) 2009
NIH - MSFA Study Section (Current Full Member and Ad Hoc) 2008-present
(MSFA: Molecular Structure and Function Panel A)
NIH – Erythrocyte/Leukocyte Biochemistry Study Section (Ad Hoc) 2008
Research Consortium (Ad Hoc)2008
Italian Center for Rare Diseases (Ad Hoc) 2007
Friedreich’s Ataxia Research Alliance (Ad Hoc)2006-present
Global Climate/Energy Fund, Stanford University (Ad Hoc) 2006
Petroleum Research Fund (Ad Hoc)2005-present
Stanford Synchrotron Radiation Laboratory (Full Member) 2001-present

REVIEWER – Peer Reviewed Journals
Antioxidants & Redox Signaling
Biochimica et Biophysica Acta
Biochemistry
Bioorganic and Medicinal Chemistry
Chemical Communications
FEBS Letters
FEMS Microbiology Letters
Human Molecular Genetics
Inorganic Chemistry
Journal of Neurological Science
Journal of the American Chemical Society
Journal of Biological Chemistry
Journal of Biological Inorganic Chemistry
Journal of Molecular Biology
Journal of Visualized Experiments
Journal of Physical Chemistry
Journal of Synchrotron Radiation
Metallomics
Molecular Nutrition and Food Research
Nature Chemical Biology
Physical Biology
Proceeding of the National Academy of Science
Science
 

Areas of Expertise

Structural Biology

Protein Spectroscopy

Molecular Biology

Chemistry

Biophysics

 

Primary Research Interest

Iron is essential for life and crucial to the human central nervous system (CNS). It is fundamental in biochemical pathways including oxidative phosphorylation, myelin synthesis, neurotransmitter production and the synthesis/metabolism of serotonin and dopamine, all of which are essential for normal CNS function. Since iron is highly reactive towards oxygen in aerobic cells, maintenance of cellular iron homeostasis is vital for normal neuronal function and for overall organism viability. Unfortunately, a growing number of human neurodegenerative disorders (Alzheimers, Huntingtons, Parkinsons, Friedreichs ataxia, etc.) have phenotypes confirming disease associated with disruption of iron homeostasis. While it is widely accepted that inflammation associated with dysfunctional iron homeostasis, accompanied by concomitant oxidative stress, is a key factor in these neurodegenerative disorders, the molecular details regarding disease related protein malfunctions are regrettably lacking. This only highlights a need for an expanded understanding of iron regulation events in the body, as this knowledge is fundamental for the development of new therapeutic approaches in the treatment of this growing class of neurodegenerative disorders. Expanding this understanding at the molecular level is the broad goal of the Stemmler laboratory.

The long-range goal of the Stemmler laboratory is to characterize the functional role proteins play in regulating cellular iron homeostasis, with special interest regarding iron-sulfur cluster (ISC) bioassembly. In eukaryotes, ISC is the major pathway for generating the iron sulfur (Fe-S) clusters used ubiquitously throughout all cells. In yeast, this pathway takes place within the mitochondria through a coordinated effort between the assembly scaffold protein (Isu1), a cysteine desulfurase (Nfs1) that provides sulfur, an accessory protein (Isd11) important in Nfs1 stabilization, an adrenodoxin (Yah1) that may provide reducing equivalents to stabilize sulfide for transfer and the iron chaperone frataxin (Yfh1). The objective of this project is to provide molecular and mechanistic details regarding interactions between these key proteins during Fe-S cluster assembly. Our central hypothesis is frataxin plays a direct role in mitochondrial Fe-S cluster assembly by serving as an iron chaperone to Isu and as a modulator of Nfs activity when bound in a stable multiprotein complex that includes Nfs/Isd11/Isu and possibly Yah.
 

Recent Publications

Peer Reviewed Original Papers: 63 Published/In Press
1. Smith, A.T.; Barupala, D.*; Stemmler, T.L.; Rosenzweig, A.C. “Discovery and characterization of a novel metal binding domain involved in cadium, cobalt, and zinc transport Nature Chemical Biology, 2015, July 20: Epub ahead of print.PMID: 26192600.
Collaborator, performed all the protein spectroscopy for the CzcP protein.
Impact Factor = 12.95

2. Bafaro, E.M.; Antala, S.; Nguyen, T.V.; Dzul, S.P.*; Doyon, B.; Stemmler, T.L.; Dempski, R.E. “The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain Metallomics, 2015, published online. PMID: 25882556.
Collaborator, performed all the XAS and ITC studies outlined within the paper.
Impact Factor = 3.978

3. Plegaria, J.S.; Dzul, S.P.*; Zuiderweg, E.R.P.; Stemmler, T.L.; Pecoraro, V.L. “Solution Structure and Stability of a De Novo Designed Peptide that Sequesters Toxic Heavy Metals Biochemistry, 2015, 54, 2858-73. Cover Article. PMID: 25790102.
Developed all experimental characterization of the peptide and trained student in these techniques.
Impact Factor = 3.38

4. Rodrigues, A.V.*; Kandegedara, A.*; Rotondo, J.A.*; Dancis, A.; Stemmler, T.L. “Iron Loading Site on the Fe-S Cluster Assembly Scaffold Protein is Distinct from the Active Site BioMetals, 2015, 28, 567-76. PMID:25782577
Original work performed in my lab.
Impact Factor = 3.28

5. Rhine, M.A.; Rodrigues, A.V.*; Urbauer, R.J.B.; Stemmler, T.L.; Harrop, T.C. “Proton-Induced Reactivity of NO- from a {CoBI}8 Complex JACS, 2014, 136,12560-3. PMID: 25073017
Collaborator, performed all the spectroscopy on model compounds.
Impact Factor = 10.68

6. Sirajuddin, S.; Barupala, D.*; Helling, S.; Marcus, K.; Stemmler, T.L.; Rosenzweig, A.C. “Effects of Zinc on Particulate Methane Monooxygenase Activity and Structure J Biol Chem, 2014, 289, 21782-94.
Contributing author, provided spectroscopic characterization of metal in protein. PMID: 24942740.
Impact Factor = 4.65

7. Hong-Hermesdorf, A.; Miethke, M.; Gallaher, S.D.; Kropat,J.; Dodani, S.C.; Barupala, D.*; Chan, J.; Domaille, D.W.; Shirasaki, D.I.; Loo, J.A.; Weber, P.K.; Pett-Ridge, J.; Stemmler, T.L.; Chang, C.J.; Merchant, S.S. “Selective sub-cellular visualization of trace metals identifies dynamic sites of Cu accumulation in Chlamydomonas Nature Chemical Biology,2014, 10, 1034-42. PMID: 25344811.
Contributing author, provided spectroscopic characterization of Cu in cells.
Impact Factor = 12.95

8. Zielazinski, E.L.: González-Guerrero, M.; Subramanian, P.*; Stemmler, T.L.; Argüello, J.M.; Rosenzweig, A.C. “Sinorhizobium meliloti Nia is a P(1B-5)-ATPase expressed in the nodule during plant symbiosis and is involved in Ni and Fe transport. Metallomics, 2013, 12, 1614-23. PMID: 22971227
Contributing author, provided spectroscopic characterization of metal during transport.
Impact Factor = 4.01

9. Pandey, A.; Gordon, D.M.; Pain, J.; Stemmler, T.L.; Dancis, A.; Pain, D. “Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly. J. Biol. Chem., 2013, 288, 36773-86. PMID: 24217246.
Original work, directly related t0 our new R01 award.
Impact Factor = 4.65

10. Leidgens, S.; Bullough, K.Z.; Shi, H.; Shakoury-Elizeh, M.; Yabe, T.; Subramanian, P.*; Hsu, E.; Natarajan, N.; Nandal, A.;Stemmler, T.L.; Philpott, C.C. “Eache member of the poly-r(C)-binding protein 1 (PCBP) family exhibits iron chaperone activity towards ferritin. J. Biol. Chem., 2013, 228, 17791-802. PMID: 23640898.
Original work, related to our discovery of the function of PCBP1.
Impact Factor = 4.65

11. Gopalasubramaniam, S.K.; Kondapalli, K.C.*; Millán –Pacheco, C.; Pastor, N.; Stemmler, T.L.; Moran, J.F.; Arredondo –Peter, R. “Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1 ScienceJet, 2013, 2, 33.
Collaborator, performed CD and XAS characterization of proteins.
Impact Factor = New online journal with no impact factor available.

12. Kowert, B.A.; Stemmler, A.J.; Stemmler, T.L.; Gentemann, S.J.; Watson, M.B.; Goodwill, V.S. “Molecular Motion of the Bis(maleonitriledithiolato)nickel Trianion in Solution J. Phys. Chem. B, 2012, 116 (26), 7687-94. PMID:22731510.
Contributing author, provided spectroscopic characterization of Ni complex by EPR.
Impact Factor = 3.607

13. Zielazinski, E.L.; Cutsail III, G.E.; Hoffman, B.M.; Stemmler, T.L.; Rosenzweig, A.C. “Characterization of a Cobalt-Specific P1B-ATPase Biochem., 2012, 51 (40), 7891-900. PMID: 22971227
Collaborator, performed XAS characterization of proteins.
Impact Factor = 3.38

14. Raimunda, D.; Subramanian, P.*; Stemmler, T.; Argüello, J.M. “A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn(2+)-ATPases Biochem. Biophys. Acta., 2012, 1818 (5), 1374-7. PMID: 22387457
Collaborator, performed XAS characterization of proteins.
Impact Factor = 3.85

15. Nandal, A.; Ruiz, J.C.; Subramanian, P.*; Ghimire-Rijal, S.*; Sinnamon, R.A.*; Stemmler, T.L.; Bruick, R.K.; Philpott, C.C. “Activation of the HIF Prolyl Hydroxylase by the Iron Chaperones PCBP1 and PCBP2 Cell Metab., 2011, 14 (5), 647-57.PMID: 22055506
Collaborator, provided all the protein necessary for experiments and performed spectroscopic
analysis of proteins.
Impact Factor = 31.96

16. Smith, S.M.; Rawat, S.*; Telser, J.; Hoffman, B.M.; Stemmler, T.L.; Rosenzweig, A.C. “Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M Biochem., 2011, 59 (1), 10231-40. PMID: 22013879
Collaborator, performed XAS characterization.
Impact Factor = 3.38

17. Ye, J.; He, Y.*; Skalicky, J.; Rosen, B.P.; Stemmler, T.L. “Resonance assignments and secondary structure predictions of the As(III) metallochaperone ArsD in solution BioMol. NMR Assn., 2011, 5 (1), 109-112. PMID: 21063813
Original work, all performed within my laboratory.
Impact Factor = 0.64

18. Cook, J.D.*; Kondapalli,K.C.*; Rawat, S.*; Childs, W.C.*; Murugesan, Y.*; Dancis, A.; Stemmler, T.L. “Molecular details of the yeast frataxin-Isu1 interaction during mitochondrial Fe-S cluster assembly Biochem., 2010, 49 (3), 8756-65. PMID: 20815377
Original work, all performed within my laboratory.
Impact Factor = 3.38

19. Traverso, M.E.; Subramanian, P.*; Davydov, R.; Hoffman, B.M.; Stemmler, T.L.; Rosenzweig, A.C. “Identification of a hemerythrin-like domain in a P1B-type transport ATPase Biochem., 2010, 49 (33), 7060-8.
Collaborator, performed XAS characterization of proteins.
Impact Factor = 3.38

20. Shin, L.; Cho, W.J.; Cook, J.*; Stemmler, T.L.; Jena, B.P. “Membrane lipids influence protein complex assembly-disassembly J. Am. Chem. Soc., 2010, 132 (16), 5596-7. PMID: 20373736
Collaborator, performed all the spectroscopy on the protein complex.
Impact Factor = 10.68

21. Yang, J.; Rawat, S.*; Stemmler, T.L.; Rosen, B.P. “Arsenic binding and transfer by the ArsD As(III) metallochaperoneBiochem., 2010, 49 (17), 3658-66.
Collaborator, performed XAS characterization of proteins.
Impact Factor = 3.38

22. Balasubramanian, R.; Smith, S.M.; Rawat, S.*; Yatsunyk, L.A.; Stemmler, T.L.; Rosenzweig, A.C. “Oxidation of methane by a biological dicopper center Nature, 2010, 465, 115-9. PMID: 20410881
Collaborator, performed XAS characterization of proteins.
Impact Factor = 22.18

23. Kondapalli, K.C.*; Bencze, K.Z.*; Dizin, E.; Cowan, J.A.; Stemmler, T.L. “NMR Assignments of a Stable Processing Intermediate of Human Frataxin BioMol. NMR Assn., 2010, 4, 61-4. PMID: 20108066
Original work, all performed within my laboratory.
Impact Factor = 0.64

24. Kowert, B.A.; Thurman-Keup, E.M.; Stemmler, A.J.; Stemmler, T.L.; Fehr, M.J.; Caldwell, C.V.; Gentemann, S.J. “Electron Spin Resonance Studies of the Reorientational Motion of Ni(mnt)2- J. Phys. Chem, B, 2010, 114, 2760-5. PMID: 20131862
Contributing author, provided spectroscopic characterization of Ni complex by EPR.
Impact Factor = 3.607

25. Kumar, R.S.; Rekhl, S.; Prabhakaran, D.; Somayazula, M.; Kim, E.; Cook, J.D.*; Stemmler, T.L.; Boothrhoyd, A.; Chance, M.R.; Cornelius, A.L. “Structural studies on Na0.75CoO2 thermoelectric material at high pressures, Solid State Comm.,2009, 149, 1712-6.
Collaborator, performed XAS characterization of complex.
Impact Factor = 1.53

26. Kandegedara, A.; Thiyagarajan, S.; Kondapalli, K.C.*; Stemmler, T.L.; Rosen, B.P. “Role of bound Zn(II) in the CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor, J. Biol. Chem., 2009, 284, 14958-65.
Collaborator, performed XAS characterization of proteins.
Impact Factor = 4.65

27. González-Guerrero, M.; Eren, E.; Rawat, S.*; Stemmler, T.L.; Argüello, J.M. “Structure of the Two Transmembrane Cu+Transport Sites of Cu+-ATPases J. Biol. Chem., 2008, 283, 29753-9. PMID: 18772137
Collaborator, performed XAS characterization of proteins.
Impact Factor = 4.65

28. Cook, J.D.*; Cho, W.J.; Stemmler, T.L.; Jena, B.P. “Circular dichroism (CD) spectroscopy of the assembly and disassembly of SNAREs: The proteins involved in membrane fusion in cells Chem. Phys. Lett., 2008, 462, 6-9. PMID: 19412345
Collaborator, performed spectroscopic characterization of protein complex.
Impact Factor = 2.15

29. Ordóñez, E.; Thiyagarajan, S.; Cook, J.D.*; Stemmler, T.L.; Gil, J.A.; Mateos, L.M.; Rosen, B.P. “Evolution of metalloid binding sites in transcriptional regulators J. Biol. Chem., 2008, 283, 25706-14. PMID: 18591244
Collaborator, performed XAS characterization of proteins.
Impact Factor = 4.65

30. Smith, S.R.; Bencze, K.Z.*; Wasiukanis, K.; Benore-Parsons, M.; Stemmler, T.L. “Investigation of the Copper Binding Site and the Role of Histidine as a Ligand in Riboflavin Binding Protein Inorg. Chem., 2008, 47, 6867-72. PMID: 18593109
Original work all performed within my laboratory through a collaborative effort.
Impact Factor = 4.59

31. Kondapalli, K.C.*; Kok, N.M.*; Dancis, A.; Stemmler, T.L. “Drosophila Frataxin: an iron chaperone during cellular [2Fe-2S] cluster bioassembly Biochem., 2008, 47, 6917-27. PMID: 18540637
Original work, all performed within my laboratory.
Impact Factor = 3.38

32. Shi, H.; Bencze, K.Z.*; Stemmler, T.L.; Philpott, C.C. “A cytosolic iron chaperone that delivers iron to ferritin Science,2008, 320, 1207-10. PMID: 18511687
Collaborator, performed all the in vitro biochemical and spectroscopic studies in our laboratory.
Impact Factor = 31.03

33. Hakemian, A.S.; Kondapalli, K.C.*; Telser, J; Hoffman, B.M.; Stemmler, T.L.; Rosenzweig, A.C. “The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b Biochem., 2008, 47, 6793-801. PMID: 18540635
Collaborator, performed XAS characterization of proteins.
Impact Factor = 3.38

34. Smith, S.R.; Bencze, K.Z.*; Wasiukanis, K.; Stemmler, T.L.; Benore-Parsons, M. “Association of Copper to Riboflavin Binding Protein; Characterization by EPR and XAS, The Open Inorg. Chem. J., 2008, 2, 39-41. PMID: 19337565
Collaborator, performed spectroscopic characterization of proteins in my laboratory.
Impact Factor = Open Access Journal so no impact factor provided.

35. Kowert, B.A.; Broeker, G.K.; Gentemann, S.J.; Stemmler, T.L.; Fehr, M.J.; Stemmler, A.J.; Thurman-Keup, E.M.; McCoo, P.W.; Everett, T.B.; Lupo, D.J.; Fitzsimmons, P.K.; Cordero, A.B. “Molecular Motion of a Nickel-bis(dithiolato) Complex in Solution, J. Phys. Chem. B, 2007, 111, 13404-9. PMID: 17979269
Contributing author, provided spectroscopic characterization of Ni complex by EPR.
Impact Factor = 3.607

36. Sazinsky, M.H.; LeMoine, B,; Orofino, M.; Davydov, R.; Bencze, K.Z.*; Stemmler, T.L.; Hoffman, B.M.; Argüello, J.M.; Rosenzweig, A.C. “Characterization and Structure of a Novel Zn2+ and [2Fe-2S]-Containing Copper Chaperone fromArchaeoglobus fulgidus, J. Biol. Chem., 2007, 282, 25950-9. PMID: 17609202
Collaborator, performed XAS characterization of protein.
Impact Factor = 4.65

37. Qin, J.; Fu, H.-L.; Ye, J.; Bencze, K.Z.*; Stemmler, T.L.; Rawlings, D. E.; Rosen, B. P. "Convergent Evolution of a New Arsenic Binding Site in the ArsR/SmtB Family of Metalloregulators", J. Biol. Chem., 2007, 282, 34346-55. PMID: 17897948
Collaborator, performed XAS characterization of protein.
Impact Factor = 4.65

38. Pastore, A.; Martin, S.R.; Politou, A.; Kondapalli, K.C.*; Stemmler, T.L.; Temussi, P.A. “Unbiased cold denaturation: low and high temperature unfolding of yeast frataxin under physiological conditions, J. Am. Chem. Soc., 2007, 129, 5374 - 5. PMID: 17411056
Collaborator, performed NMR characterization of protein.
Impact Factor = 10.68

39. Bencze K.Z.*; Yoon, T.; Bradley, P.B.*; Cowan, J.A.; Stemmler, T.L. “Human frataxin iron structure and ferrochelatase binding interface, Chem. Comm., 2007, 18, 1798-800. PMID: 17476391
Original work, performed in my laboratory.
Impact Factor = 6.38

40. Lieberman, R.L.; Kondapalli,K.C.*; Shrestha, D.B.; Hakemian, A.S.; Smith, S.M.; Telser, J.; Kuzelka, J.; Gupta, R.; Borovik, A.S.; Lippard, S.J.; Hoffman, B.M.; Rosenzweig, A.C.; Stemmler, T.L. “Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy, Inorg. Chem., 2006, 45, 8372-81. PMID: 16999437
Original work, performed in my laboratory.
Impact Factor = 4.59

41. Cook, J.D.*; Bencze, K.Z.*; Jankovic, A.*; Crater, A.K.*; Busch, C.*; Bradley, P.B.*; Spaller, M.; Stemmler, T.L.“Monomeric yeast frataxin is an iron binding protein, Biochem., 2006, 45, 7767-77. PMID: 16784228
Original work, performed in my laboratory.
Impact Factor = 3.38

42. Meroueh, S.O.; Bencze, K.Z.*; Hesek, D.; Lee, M.; Fisher, J.F.; Stemmler, T.L.; Mobashery, S. “Three-Dimensional Structure of Bacterial Cell Wall Peptidoglycan, Proc. Natl. Acad. Sci, U.S.A., 2006, 103, 4404-9. PMID: 16537437
Collaborator, performed NMR characterization of molecule.
Impact Factor = 9.74

43. Hakemian, A.S.; Tinberg, C.E.; Kondapalli, K.C.*; Tesler, J.; Hoffman, B.M.; Stemmler, T.L.; Rosenzweig, A.C. “The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I), J. Am. Chem. Soc., 2005,127, 17142-3. PMID: 16332035
Collaborator, performed XAS characterization of protein.
Impact Factor = 10.68

44. Xu, X.; Kona, F.; Wang, J.; Lu, J.; Stemmler, T.L.; Gatti, D.L. “The catalytic and conformational cycle of Aquifex aeolicus KDO8P synthase: role of the L7 loop, Biochem., 2005, 44, 12434-44.
Collaborator, performed NMR characterization of protein.
Impact Factor = 3.38

45. He, Y.*; Alam, S.L.; Proteasa, S.V.*; Zhang, Y.*; Lesuisse, E.; Dancis, A.; Stemmler, T.L. “Yeast Frataxin Solution Structure, Iron Binding and Ferrochelatase Interaction, Biochem., 2004, 43, 16254-62. PMID: 15610019
Original work, performed entirely in my laboratory.
Impact Factor = 3.38

46. Golemi-Kotra, D.; Meroueh, SO; Kim, C; Vakulenko, SB; Bulychev, A; Stemmler, A.J.; Stemmler, T.L.;Mobashery, S. “The Importance of a Critical Protonation State and the Fate of the Catalytic Steps in Class A b-Lactamases and penicillin-binding proteins, J. Biol. Chem, 2004, 273, 34665-73. PMID: 15152012
Collaborator, performed NMR characterization of protein.
Impact Factor = 4.65

47. Ramírez-Solís, A.; Mukopadhyay, R.; Rosen, B.P.; Stemmler, T.L. “Experimental and Theoretical Characterization of Arsenite in Water: Insights into the Coordination Environment of As-O, Inorg. Chem., 2004, 43, 2954-9. PMID: 15106984
Original work, performed entirely in my laboratory.
Impact Factor = 4.59

48. Lieberman, R.L.; Rosenzweig, A.C.; Stemmler, T.L. “Structural Insight into the Metal Active Site of Methane Monooxygenase – an Enzyme that Converts Methane to Methanol Stanford Synchrotron Radiation Laboratory Highlights, 2003, E-published at http://www-ssrl.slac.stanford.edu/research/highlights_archive/pmmo.html.
Collaborator, performed XAS characterization of protein.

49. Wang, B.; Alam S.L.; Meyer H.H.; Payne M.; Stemmler, T.L.; Davis D.R.; Sundquist W.I. “Structure and Ubiquitin interactions of the conserved NZF domain of Npl4. J. Biol. Chem., 2003, 278, 20225-34. PMID: 12644454
Collaborator, performed XAS characterization of protein.
Impact Factor = 4.65

50. Lieberman, R.L.; Shrestha, D.B.; Doan, P.E.; Hoffman, B.M.; Stemmler, T.L.; Rosenzweig, A.C. “Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster, Proc. Natl. Acad. Sci, U.S.A., 2003, 100, 3820-3825.
Collaborator, performed XAS characterization of protein.
Impact Factor = 9.74

51. Baldwin, M.J.; Law, N.A.; Stemmler, T.L.; Kampf, J.W.; Penner-Hahn, J.E.; Pecoraro, V.L. “Reactivity of [{MnIV(salpn)}2(m-O,m-OCH3)]+ and [{MnIV(salpn)}2(m-O,m-OH)]+: Effects of Proton Lability and Hydrogen Bonding Inorg. Chem, 1999, 38, 4801-4809.
Graduate studies, performed spectroscopic characterization of molecule.
Impact Factor = 4.59

52. Brunold T.C.; Gamelin, D.R.; Stemmler, T.L.; Mandal, S.K.; Armstrong, W.H.; Penner-Hahn, J.E.; Solomon, E.I. “Spectroscopic Studies of Oxidized Manganese Catalase and Oxo-Bridged Dimanganese(III) Model Complexes: Electronic Structure of the Active Site and Its Relation to Catalysis J. Am. Chem. Soc., 1998, 120, 8724-8738.
Graduate studies, performed spectroscopic characterization of molecules.
Impact Factor = 10.68

53. Schwedler, U.v.; Stemmler, T.L.; Klishko, V.Y.; Albertine, K.H.; Davis, D.R. .; Sundquist, W.I. “Proteolytic Refolding of the HIV-1 Capsid Protein Amino-terminus Facilitates Viral Core Assembly, EMBO J.,1998, 17, 1555-1568.
Post-Doc, performed NMR characterization of proteins.
Impact Factor = 9.82

54. Kowert, B.A.; Stemmler, T.L.; Fehr, M.J.; Sheaff, P.J.; Gillum, T.J.; Dang, N.C.; Hughs, A.M.; Staggemeier, B.A.; Zavich, D.V. “Studies of the Translational and Reorientational Motions of Planer Nickel Complex Ions, J. Phys. Chem. B, 1997, 101, 8662-8666.
Undergraduate studies, performed EPR characterization of molecules.
Impact Factor = 3.607

55. Stemmler, T.L.; Sturgeon, B.E.; Randall, D.W.; Britt, R.D.; Penner-Hahn, J.E. “Spectroscopic Characterization of Inhibitor Interactions with the Mn(III)Mn(IV) Core in Lactobacillus plantarum Manganese Catalase, J. Am. Chem. Soc.,1997, 119, 9215-9225.
Graduate studies, performed all characterization studies of molecules.
Impact Factor = 10.68

56. Stemmler, T.L.; Sossong, T.R.; Ash, D.E.; Elgren, T.; Kurtz, D.; Penner-Hahn, J.E. “EXAFS Comparison of the Dimanganese Core Structure of Manganese Catalase, Arginase and Manganese-Substituted Ribonucleotide Reductase and Hemerythrin, Biochem., 1997, 36, 9847-9858.
Graduate studies, performed all characterization studies of molecules.
Impact Factor = 3.38

57. Kowert, B.A.; Higgins, E.J.; Mariencheck, W.I.; Stemmler, T.L.; Kantorovich, V. “Electron Spin Resonance Studies of Reorientational Motion in Glass-Forming Liquids, J. Phys. Chem. B, 1996, 100, 11211-11216.
Undergraduate studies, performed EPR characterization of molecules.
Impact Factor = 3.607

58. Grush, M.M.; Chen, J.; Stemmler, T.L.; Ralston, C.; George, S.J.; Gelasco, A.; Penner-Hahn, J.E.; Christou, G.; Cramer, S.P. “Manganese L-Edge X-Ray Absorption Spectroscopy of Manganese Catalase from L. plantarum and Mixed Valence Manganese Complexes, J. Am. Chem. Soc., 1996, 118, 65-69.
Graduate studies, performed spectroscopic characterization of molecules.
Impact Factor = 10.68

59. Stemmler, T.L.; Barnhart, T.M.; Penner-Hahn, J.E.; Tucker, C.E.; Knochel, P.; Böhme, M.; Frenking, G. “Structural Characterization of Organocuprate Reagents. EXAFS Spectroscopy and Ab Initio Calculations, J. Am. Chem. Soc., 1995, 117, 12489-97.
Graduate studies, performed all characterization studies of molecules.
Impact Factor = 10.68

60. Baldwin, M.J.; Stemmler, T.L.; Riggs-Gelasco, P.J.; Kirk, M.L.; Penner-Hahn, J.E.; Pecoraro, V.L. “Structural and Magnetic Effects of Successive Protonations of Oxo Bridges in High-Valent Manganese Dimers, J. Am. Chem. Soc.,1994, 116, 11349-56.
Graduate studies, performed spectroscopic characterization of molecules.
Impact Factor = 10.68

61. Tesmer, J.J.G.; Stemmler, T.L.; Penner-Hahn, J.E.; Davisson, V.J.; Smith, J.L. “Preliminary X-Ray Analysis ofEscherichia coli GMP Synthetase: Determination of Anomalous Scattering Factors for a Cysteinyl Mercury Derivative,Proteins: Structure, Function, and Genetics, 1994, 18, 394-403.
Graduate studies, performed spectroscopic characterization of molecules.
Impact Factor = 3.34

62. Gamelin, D.R.; Kirk, M.L.; Stemmler, T.L.; Pal, S.; Armstrong, W.H.; Penner-Hahn, J.E.; Solomon, E.I. “Electronic Structure and Spectroscopy of Manganese Catalase and Di-µ-oxo [Mn(III/IV)] Model Complexes, J. Am. Chem. Soc., 1994, 116, 2392-99.
Graduate studies, performed spectroscopic characterization of molecules.
Impact Factor = 10.68

63. Stemmler, T.; Penner-Hahn, J.E.; Knochel, P. “Structural Characterization of Organocopper Reagents by EXAFS Spectroscopy, J. Am. Chem. Soc., 1993, 115, 348-50.
Graduate studies, performed all characterization studies of molecules.
Impact Factor = 10.68

Reviews (6 Published)
1. Subramanian, P.*; Rodrigues, A.*; Ghimire, S.R.*; Stemmler, T.L. “Iron chaperones for mitochondrial Fe-S cluster biosynthesis and ferritin iron storage Cur. Opin. Chem. Biol., 2011, 15, 312-8. PMID: 21288761
Review written entirely by my laboratory.
Impact Factor = 9.47

2. Rawat, S.*; Stemmler, T.L. “Key players and their role during mitochondrial Fe-S cluster biosynthesis Chem. Eur. J., 2011, 17,746-753. PMID: 21226084
Review written entirely by my laboratory.
Impact Factor = 5.83

3. Stemmler, T.L.; Lesuisse, E.; Pain, D.; Dancis, A. “Frataxin and mitochondrial Fe-S cluster biogenesis J. Biol. Chem., 2010, 285 (35), 26737-43.
I wrote large sections and played a major role in putting the review together.
Impact Factor = 4.65

4. Cook, J.D.*; Penner-Hahn, J.E.; Stemmler, T.L. “Structure and dynamics of metalloproteins in live cells, Method. Cell. Biol., 2009, 90, 199-216. PMID: 19195552
Review directed by Stemmler after writing most of the text.
Impact Factor = 1.44

5. Bencze, K.Z.*; Kondapalli, K.C.*; Cook, J.D.*; McMahon, S.*; Millan-Pacheco, C.; Pastor, N.; Stemmler, T.L. “The structure and function of frataxin, Crit. Rev. of Biochem. & Mol. Biol., 2006, 41, 269-91. PMID: 16911956
Review written entirely in my laboratory.
Impact Factor = 5.58

6. Riggs-Gelasco, P.J.; Stemmler, T.L.; Penner-Hahn, J.E. “XAFS of Dinuclear Metal Sites in Proteins and Model Compounds, Coord. Chem. Review, 1995, 114, 245-86.
Review written in part (33%) by Stemmler during his graduate work.
Impact Factor = 11.02

Book Chapters (2 Published, 1 In Press)
1. Dzul, S.P.*; Stemmler, T.L.; Penner-Hahn, J.E. “Manganese Proteins with Mono- and Dinuclear Metal Sites in The Encyclopedia of Inorganic Chemistry, Robert A. Scott Eds., Chichester, UK: John Wiley & Sons, Ltd., 2015, In Press.
Chapter written predominately by my laboratory.

2. Kondapalli, K.C.*; Dancis, A.; Stemmler, T.L. “Molecular interaction between Frataxin and Ferrochelatase during Heme Assembly in Bioinorganic Chemistry; Cellular Systems and Synthetic Models, ACS Symposium Series 1012, Eric C. Long and Michael J. Baldwin, Eds., American Chemical Society, 2009, 17-30.
Chapter written almost entirely within my laboratory.

3. Bencze, K.Z.*; Kondapalli, K.C.*; Stemmler, T.L. “X-ray Absorption Spectroscopy in Applications of Physical Methods to Inorganic and Bioinorganic Chemistry, Robert A. Scott and Charles M. Lukehart Eds., Chichester, UK: John Wiley & Sons, Ltd., 2008, 513-28.
Chapter written entirely in my laboratory.
 

Research Connect link

https://researchconnect.wayne.edu/en/persons/timothy-stemmler

Laboratory Web Site

Stemmler Lab

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