Timothy Stemmler

Suffix

Ph.D.

Office Location

EACPHS, Room 3138

Phone

313-577-5712

Department

Pharmaceutical Sciences

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, Ann Arbor 1996
• Master of Science, Physical Chemistry, St. Louis University, St. Louis, MO 1990
• Bachelor of Arts, Physical Chemistry, St. Louis University, St. Louis, MO 1989

Positions and Employment

• Interim Vice President for Research, Wayne State University 2022 - present

Previous appointments

• Associate Dean for Research, Eugene Applebaum College of Pharmacy and Health Sciences
• Professor and Director of Research, Department of Pharmaceutical Sciences
• Associate Dean for Postdoctoral Studies
• Adjunct Professor, Department of Biochemistry and Molecular Biology
• Associate Chair of Pharmaceutical Sciences, Wayne State University 2016 - 2017
• Assistant Dean of the Graduate School, Wayne State University 2014 - 2017
• Director of Research, Dept. of Pharm Sci, Wayne State University 2013 - 2016
• Adjunct Professor of Biochemistry and Molecular Biology, Wayne State University 2013 - present
• Professor of Biochemistry and Molecular Biology, Wayne State University 2012 - 2013
• Associate Professor of Biochemistry and Molecular Biology, Wayne State University 2007 - 2012
• Adjunct Associate Professor of Pharm Sci., Wayne State University 2007 - 2012
• Visiting Professor, Stanford University, Stanford Synchrotron Radiation Lightsource 2012
• Adjunct Assistant Professor of Pharm Sci., Wayne State University 2003 - 2007
• Assistant Professor of Biochemistry & Molecular Biology, Wayne State University 2000 - 2007

Awards and Honors

• Distinguished Graduate Faculty Award 2019
• Director of Postdoctoral Office, WSU 2014-present
• Associate Chair of Pharmaceutical Sciences, WSU 2016-2017
• Asst. Dean of Grad School, Dir of Postdoctoral Studies 2015 - 2017
• Director of Research for the Dept. of Pharmaceutical Sciences 2013 - 2016
• SOM Faculty Research Excellence Award 2011
• SOM College Teaching Award 2010
• Career Development Award 2011
• Academy of Scholars, Junior Faculty Inductee, WSU 2007
• SOM Faculty Research Excellence Award 2006
• SOM College Teaching Award 2005
• 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
• Leapold Marcus Undergraduate Research Award, St. Louis University 1989
• Eagle Scout 1981

Professional Memberships

REVIEWER – Grants

• German Research Foundation (DFG) 2016
• French National Research Agency (ANR) 2016
• NIH – ZRG1 BCMB-D (02)M Special Emphasis Panel 2016 - present
• NIH – BMR-IRB Special Emphasis Panel 2015
• NIH – ZRG1 BCMB-U (40)P (Ad Hoc) 2015
• NSF – Biomolecules Study Section (Ad Hoc) 2009 - present
• Friedreich’s Ataxia Research Alliance (Ad Hoc) 2006 - present
• Petroleum Research Fund (Ad Hoc) 2005 - present
• Stanford Synchrotron Radiation Laboratory (Full Member) 2001 - present
• Czech Science Foundation 2013 - 2014
• NIH – ZGM1 TRN-A Special Emphasis Study Section (Ad Hoc) 2012 - 2013
• United Kingdom Ataxia Foundation 2012
• NIH – ZHD1 Special Emphasis Study Section (Ad Hoc) 2011
• NIH – ZRG1 Special Emphasis Study Section (Ad Hoc) 2011, 2014
• Fonds québécois de la recherche sur la nature ET les technologies (Ad Hoc) 2010
• Montreal, Canada
• NIH – P41 SSRL Facility Grant Study Section (Full Member) 2009
• NIH - MSFA Study Section (Ad Hoc then Current Full Member) 2008 - 2014
• (MSFA: Molecular Structure and Function Panel A)
• NIH – Erythrocyte/Leukocyte Biochemistry Study Section (Ad Hoc) 2008
• Research Corporation (Ad Hoc) 2008
• Italian Center for Rare Diseases (Ad Hoc) 2007
• Global Climate/Energy Fund, Stanford University (Ad Hoc) 2006

REVIEWER – Peer Reviewed Journals

• Antioxidants & Redox Signaling
• Archives of Biochemistry and Biophysics
• Biochimica et Biophysica Acta
• Biochemistry
• Biochemie
• Bioorganic and Medicinal Chemistry
• Chemical Communications
• Environmental Science and technology
• 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 Inorganic Biochemistry
• Journal of Molecular Biology
• Journal of Visualized Experiments
• Journal of Physical Chemistry
• Journal of Synchrotron Radiation
• Metallomics
• Molecular Microbiology
• Molecular Nutrition and Food Research
• Nature Chemical Biology
• Physical Biology
• Proceeding of the National Academy of Science, USA
• Science

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: 77 Published

1. Purohit, R.; Ross, M.O.; Batelu, S,*; Kusowski, A.*; Stemmler, T.L.; Hoffman, B.M.; Rosenzweig, A.C. “A Cu+-specific CopB transporter: Revising P1B-type ATPase classification.” Proc. Natl. Acad. Sci, U.S.A., 2018, 115. 2108-13. PMID: 29440418.
Collaborator, performed XAS characterization of protein.
Impact Factor = 9.74

2. Holcomb, J.; Doughan, M.; Spellmon, N.; Lewis, B.*; Perry, E.; Zhang, Y.; Nico, L.; Wan, J.; Chakravarthy, S.; Shang, W.; Miao, Q.; Stemmler, T.L.; Yang, Z. “SAXS analysis of a soluble cytosolic NgBR construct including extracellular and transmembrane domains.” Plos One, 2018, Published Online, https://doi.org/10.1371/journal.pone.0191371.
Impact Factor = 3.54

3. Pawitwar, S.; Nadar, V.; Kandegedara, A.*; Stemmler, T.L.; Rosen, B.; Yoshinaga, M. “Biochemical characterization of ArsI: a novel C-As lyase for degradation of environmental organoarsenicals.” Environmental Science and Technology, 2017, 51, 11115-25. PMID:28936873.
Contributing author, provided spectroscopic characterization of protein.
Impact Factor = 5.39

4. Truong, P.T.; Gale, E.M.; Dzul, S.P.*; Stemmler, T.L.; Harrop, T.C. “Steric Enforcement about One Thiolate Donor Leads to New Oxidation Chemistry in a NiSOD Model Compound. ” Inorganic Chemistry, 2017, 56, 7761-80. PMID: 28459242
Contributing author, provided spectroscopic characterization of compound.
Impact Factor = 4.59

5. Ruetz, M.; Kumutima, J.; Lewis, B.E.*; Filipovic, M.R.; Lehnert, N.; Stemmler, T.L.; Banerjee, R. “A Distal Ligand Mutes the Interaction of Hydrogen Sulfide with Human Neuroglobin.” J. Biol. Chem., 2017, 292, 6512-28. PMID: 28246171.
Contributing author, provided spectroscopic characterization of metal in protein.
Impact Factor = 4.65

6. Steiner, R.A.; Dzul, S.P.*; Stemmler, T.L.; Harrop, T.C. “Synthesis and Speciation-Dependent Properties of a Multimetallic Model Complex of NiSOD That Exhibits Unique Hydrogen-Bonding” Inorganic Chemistry, 2017, 56, 2849-62. PMID: 28212040
Contributing author, provided spectroscopic characterization of compound.
Impact Factor = 4.59

7. Das, B.; Kandegedara, A.*; Xu, L.; Antonio, T.; Stemmler, T.L.; Reith, M.E.A.; Dutta, A.K. “A Novel Fe(II) Preferring Dopamine Agonist Chelator as Potential Symptomatic and Neuroprotective Therapeutic gent for Parkenson’s Disease.” ACS Chemical Neuroscience, 2017, 8, 723-30. DOI: 10.1021/acschemneuro.6b00356
Contributing author, provided spectroscopic characterization of compound.
Impact Factor = 4.36

8. Mahapatra, G.; Varughese, A.; Ji, Q.; Lee, I.; Liu, J.; Vaishnav, A.; Sinkler, C.; Kapralov, A.A.; Moraes, C.T.; Sanderson, T.H.; Stemmler, T.L.; Grossman, L.I.; Kagan, V.E.; Brunzelle, J.S.; Salomon, A.R.; Edwards, B.F.; Hüttemann, M. “Phosphorylation of Cytochrome c Threonine 28 Regulates Electron Transport Chain Activity in Kidney: Implications for AMP Kinase.” J. Biol. Chem., 2017, 292, 64-79. PMID: 27758862.
Contributing author, provided spectroscopic characterization of metal in protein.
Impact Factor = 4.65

9. Dzul, S.*; Rocha, A.; Rabat, S.; Kandegedara, A.*; Kusowski, A.*; Pain, J.; Murari, A.; Pain, D.; Dancis, A.; Stemmler, T.L.; “In vitro characterization of a novel Isu homologue from Drosophila melanogaster for de novo FeS-cluster formation.” Metallomics, 2017,9, 48-60. PMID: 27738674.
This work in predominately original from our laboratory.
Impact Factor = 3.54

10. Walter, M.R.; Dzul, S.P.*; Rodrigues, A.V.*; Stemmler, T.L.; Tesler, J.; Conradie, J.; Ghosh, A.; Harrop, T.C. “Synthesis of Co(II)-NO(-) Complexes and their reactivity as a Source of Nitroxyl” J. Am. Chem. Soc., 2016, 138, 12459-71. PMID: 27562882.
Collaborator, performed XAS characterization of Myoglobin Samples.
Impact Factor = 10.68

11. Bostelaar, T.; Vitvitsky, V.; Kumutima, J.; Lewis, B.E.*; Yadav, P.K.; Brunold, T.C.; Filipovic, M.; Lehnert, N.; Stemmler, T.L.; Banerjee, R. “Hydrogen Sulfide Oxidation by Myoglobin” J. Am. Chem. Soc., 2016, 138, 8476-88. PMID: 27310035.
Collaborator, performed XAS characterization of Myoglobin Samples.
Impact Factor = 10.68

12. Patel, S.J.; Lewis, B.E.*; Long, J.E.; Nambi, S.; Sassetti, C.M.; Stemmler, T.L.; Arguello, J.M. “Fine Tuning of Substrate Affinity Leads to Alternative Roles of Mycobacterium tuberculosis Fe(III) ATPases” J. Biol. Chem., 2016, 291, 4700-5. PMID: 27022029
Contributing author, provided spectroscopic characterization of metal in protein.
Impact Factor = 4.65

13. Shimberg, G.D.; Michalek, J.L.; Oluyadi, A.D.; Rodrigues, A.V.*; Beth E. Zucconi, B.E.; Neu, H.; Ghosh, S.; Sureschandra, K.; Wilson, G.M.; Stemmler, T.L.; Michel, S.L.J. “Cleavage and Polyadenylation Specificity Factor 30: An RNA binding Zinc Finger Protein with an unexpected 2Fe-2S cluster” Proc. Natl. Acad. Sci, U.S.A., 2016, 113, 4700-5. PMID: 27071088.
Collaborator, performed XAS characterization of protein.
Impact Factor = 9.74

14. Kumar, N.V.; Yang, J.; Pillai, J.K.; Rawat, S.*; Solano, C.; Kumar, A.; Grotli, M.; Stemmler, T.L.; Rosen, B.P.; Tamas, M.K. “Arsenic directly binds to and activates the yeast AP-1-like transcription factor Yap8” Molecular and Cellular Biology, 2015, 36, 913-922. PMID: 26711267
Contributing author, provided spectroscopic characterization of metal in protein.
Impact Factor = 4.78

15. 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, 11, 678-84. PMID: 26192600.
Collaborator, performed all the protein spectroscopy for the CzcP protein.
Impact Factor = 12.95

16. 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, 7, 1319-30. PMID: 25882556.
Collaborator, performed all the XAS and ITC studies outlined within the paper.
Impact Factor = 3.978

17. 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

18. 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

19. 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” J. Am. Chem. Soc., 2014, 136,12560-3. PMID: 25073017
Collaborator, performed all the spectroscopy on model compounds.
Impact Factor = 10.68

20. 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. PMID: 24942740.
Contributing author, provided spectroscopic characterization of metal in protein.
Impact Factor = 4.65

21. 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

22. 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

23. 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

24. 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

25. 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.

26. 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

27. 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

28. 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

29. 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

30. 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

31. 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

32. 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

33. 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

34. 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

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

36. 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

37. 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

38. 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

39. 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

40. 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

41. 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

42. 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

43. 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

44. 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

45. 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

46. 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

47. 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

48. 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.

49. 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

50. 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 from Archaeoglobus fulgidus,” J. Biol. Chem., 2007, 282, 25950-9. PMID: 17609202
Collaborator, performed XAS characterization of protein.
Impact Factor = 4.65

51. 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

52. 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

53. 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

54. 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

55. 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

56. 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

57. 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

58. 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

59. 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

60. 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 -Lactamases and penicillin-binding proteins,” J. Biol. Chem, 2004, 273, 34665-73. PMID: 15152012
Collaborator, performed NMR characterization of protein.
Impact Factor = 4.65

61. 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

62. 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.

63. 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

64. 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

65. Baldwin, M.J.; Law, N.A.; Stemmler, T.L.; Kampf, J.W.; Penner-Hahn, J.E.; Pecoraro, V.L. “Reactivity of [{MnIV(salpn)}2(-O,-OCH3)]+ and [{MnIV(salpn)}2(-O,-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

66. 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

67. 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

68. 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

69. 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

70. 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

71. 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

72. 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

73. 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

74. 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

75. Tesmer, J.J.G.; Stemmler, T.L.; Penner-Hahn, J.E.; Davisson, V.J.; Smith, J.L. “Preliminary X-Ray Analysis of Escherichia 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

76. 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

77. 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 (7 Published)

1. Barupala, D.P.*; Dzul, S.P.*; Riggs-Gelasco, P.J.; Stemmler, T.L. “Synthesis, Delivery and Regulation of Eukaryotic Heme and Fe-S Cluster Cofactors” Archives In Biochem. and Biophys., 2016, 15, 60-75. PMID: 26785297
Review written almost entirely by my laboratory.
Impact Factor = 3.02

2. 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

3. 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

4. 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

5. 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

6. 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

7. 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 (3 Published)
1. Dzul, S.P.*; Stemmler, T.L.; Penner-Hahn, J.E. “Manganese Proteins with Mono- and Dinuclear Metal Sites” in Encyclopedia of Inorganic and Bioinorganic Chemistry, Robert A. Scott Eds., Chichester, UK: John Wiley & Sons, Ltd., 2015, 1-11.
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.

Laboratory Web Site

Stemmler Lab

DO NOT EDIT: Experts guide blurb

Tim Stemmler is examining the role proteins play in regulating cellular iron homeostasis, the disruption of which can cause human neurodegenerative disorders including Alzheimer’s, Huntington’s, Parkinson’s and Friedreichs Ataxia.

Research Description

Affiliated Departments

• Pharmaceutical Science