Prof. Sharon Ruthstein
Sharon Ruthstein gained her B.Sc in Chemical Engineering from the Technion, Haifa, Israel. Then she continued her graduate studies in the Chemistry Department at Weizmann Institute of Science, Rehovot, Israel. She achieved her PhD under the superviosion of Prof. Daniella Goldfarb. After graduating from the Weizmann Institute in 2008, she became an EMBO Postdoctoral Fellow at the University of Pittsburgh, where she worked under the supervision of Prof. Sunil Saxene.
Prof. Ruthstein joined the Department of Chemistry at Bar-Ilan University in October 2011. Her research is aiming to exploit biological pathways in human and bacteria cells, which involve metal ions, using pulsed Electron Paramagnetic Resonance Spectroscopy (EPR).
2008-2011 EMBO Long-term Post-doctoral Fellow at the
University of Pittsburgh, Department of Chemistry.
Advisor: Prof. Sunil Saxena.
2003-2008 Ph.D. in Chemistry, with Honors, Weizmann Institute of Science,
Israel. Advisor: Prof. Daniella Goldfarb.
2000-2003 M.Sc in Chemistry, with Honors, Weizmann Institute of Science.
1996-2000 B.Sc in Chemical Engineering, (summa cum laude),
Technion, Haifa, Israel.
2017 - present: Associate Profeesor, Department of Chemistry, Bar-Ilan University.
2011- 2017: Senior Lecturer, Department of Chemistry, Bar-Ilan University.
Awards and Fellowships
2017 ICS Young Scientist award
2017 ERC - STG
2015 Krill award (Wolf Foundation)
2008 EMBO Long-term Fellowship for post-doctoral studies.
2008 AAUW Post-doctoral fellowship – declined upon receiving the
2007 Dean's Excellence Prize for Ph.D. – Weizmann Institute of Science.
2007 JEOL Student Prize
2007 Auto Schwartz Prize – Weizmann Institute of Science.
2007 Wolf Foundation Fellowship for Excellent Ph.D. Students.
2004 Eshkol Scholarship for Ph.D. students, Jerusalem, Israel.
2003 Mention of Honor of the Knesset (The Israeli Parliament).
2003 Dean's Excellence Prize for M.Sc. – Weizmann Institute of Science,
1998 Sidney Goldstein Excellence Prize – Technion, Haifa, Israel.
- Shenberger, Y.; Marciano, O.; Gottlieb, H.; Ruthstein, S.; Insights into the N-terminal Cu(II) and Cu(I) binding sites of the human copper transporter Ctr1. J. Coord. Chem. 2018, in press.
- Levy, A.; Turgeman, M.; Gevorkyan-Aiapetov, L.; Ruthstein, S.; The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations. Protein Sci. 2017, 26, 1609-1618.
- Meir, A.; Abdelhai, A.; Moskovitz, Y.; Ruthstein, S.; EPR spectroscopy targets conformational and topological changes in the E.coli membrane fusion CusB dimer upon Cu(I) binding. Biophys. J. 2017, 112, 2494-2502.
- Sameach, H.; Narunsky, A.; Azoulay-Ginsburg, S.; Gevorkyan-Aiapetov, L.; Zehavi, Y.; Moskovitz, Y.; Juven-Gershon, T.; Ben-Tal, N.; Ruthstein, S.; Structural and dynamics characterization of the MerR family metalloregulator CueR in its repression and activation states. Structure. 2017, 25, 988-996.
- Levy, A.; Nissim, M.; Mendelman, N.; Chill, J.; Ruthstein, S.; Ctr1 intracellular loop is involved in the copper transfer mechanism to the Atox1 metallochaperone. J. Phys. Chem. B. 2016, 120, 12334-12345.
- Marciano, O.; Gonen, S; Levy, N.; Yemini, R; Nessim, G.; Ruthstein, S.; Elbaz, L.; Modulation of oxygen content in graphene surfaces using temperature programmed reductive annealing: electron paramagnetic resonance (EPR) and electrochemical study. Langmuir, 2016, 32, 11672-11680.
- Zer-Aviv, P.; Shubely, M.; Moskovitz, Y.; Viskind, O.; Albeck, A.; Vertommen, D.; Ruthstein, S.; Shokhen, M.; and Gruzman, A. . A new oxopiperazin-based peptidomimetic molecule inhibits prostatic acid phosphatase secretion and induces prostate cancer cells apoptosis. Chemistry Select, 2016, 1, 4658-4667.
- Fleker, O.; Borenstein, A.; Lavi, R.; Ruthstein, S.; Aurbach D.; Preparation and properties of metal organic framework/activated carbon composite materials. Langmuir. 2016, 32, 4935-4944.
- Shilina, Y.; Ziv, B.; Meir, A.; Banerjee, A.; Ruthstein, S.; Luski, S.; Aurbach, D.; Halalay, I.C.; Combined EPR and AAS/ICP analysis as diagnostics for soluble maganese species from Mn-based positive electrode materials in Li-ion cells. Anal. Chem. 2016, 88, 4440-4447.
- Marciano, O.; Moskovitz, Y.; Hamza, I.; Ruthstein, S.; Histdine residues are important for preserving the structure and heme binding to the c.elegans HRG-3 heme trafficking protein. J. Biol. Inorg. Chem. 2015, 20, 1253-1261.
- Weintraub, S.; Moskovitz, Y.; Fleker, O.; Levy, A.; Meir, A.; Ruthstein, S.; Benisvy, L.; Gruzman, A.; SOD mimetic activity and antiproliferative properties of a novel tetra nuclear copper(II) complex. J. Biol. Inorg. Chem. 2015, 20, 1287-1298.
- Dalalyon, A.; Qi, M.; Ruthstein, S.; Vega, S.; Godt, A.; Feintuch, A.; Goldfarb, D.; Gd(III)-Gd(III) EPR distance measurments - the range of accessible distances and the impact of zero field splitting. PCCP, 2015, 17, 18464-18476.
- Meir, A.; Natan, A.; Moskovitz, Y.; Ruthstein, S.; EPR spectroscopy identifies Met and Lys rediues that are essential for the interaction between CusB N-terminal domain and the metallochaperone CusF. Metallomics, 2015, 7, 1163-1172.
- Shenberger, Y.; Shimshi, A.; Ruthstein, S.; EPR spectroscopy shows that the blood carrier protein, human serum albumin, closley interacts with the N-terminal domain of the copper transporter, CTR1. J. Phys. Chem. B. 2015, 119, 4824-4830.
- Shenberger, Y.; Gottlieb, H.; Ruthstein, S.; EPR and NMR spectroscopies provide input on the coordination of Cu(I) and Ag(I) to a disordered methionine segment. J. Biol. Inorg. Chem. 2015, 20, 719-727.
- Ruthstein, S.; Ji, M.; Shin, B.K.; Saxena, S.; A simple double quantum coherence ESR sequence that minimizes nuclear modulation in Cu(II)-ion based distance measurments. J. Magn. Reson. 2015, 257, 45-50.
- Munder, A.; Moskovitz, Y.; Rediko, B.; Levy, A.; Ruthstein, S.; Gellerman, G.; Gruzman, A.; Antiproliferative Effects of Novel Aminoacridine-Based Compounds. Med. Chem. 2015. 11, 373-382.
- Levy, A.; Yarmiayev, V.; Moskovitz, Y.; Ruthstein, S.; Probing the Structural Flexibility of the Human Copper Metallochaperone Atox1 Dimer and its Interaction with the CTR1 C-Terminal Domain. J. Phys. Chem. B. 2014, 118, 5832-5842.
- Green, U.; Keinan-Adamsky, K.; Attia, S.; Aizenshtat, Z.; Goobes, G.; Ruthstein, S.; Cohen, H.; Elucidating the role of stable carbon radicals in the low temperature oxidation of coals by coupled EPR-NMR spectroscopy - a method to characterize surfaces of porous carbon radicals. PCCP. 2014, 16, 9364-9370.
- Green, U.; Shenberger, Y.; Aizenshtat, Z.; Cohen, H. Ruthstein, S.; Exploring the radical nature of a carbon surface by Electron Paramagnetic resonance and a calibrated gas flow. JoVE, 2014, .86, doi:10.3791/51548.
- Ji, M.; Ruthstein, S.; Saxena, S.; Paramagnetic metal ions in Pulsed ESR distance measurements. Acc. Chem. Res. 2014, 47, 688-695.
- Rubinovich, L.; Ruthstein, S.; Weiss, D.; The Arabidopsis cysteine-rich GASA5 is a redox-active metalloprotein that suppresses gibberellin responses. Mol. Plant. 2014, 7(1), 244-247.
- Shenberger, Y.; Yarmiayev, V.; Ruthstein, S.; Exploring the interaction between the human copper transporter, CTR1, c-terminal domain and a methionine motif, in the presence of Cu(I) and Ag(I) ions, using EPR spectrosopy. Mol. Phys. 2013, 111, 2980-2991.
- Ruthstein,S.; Ji, M.; Mehta, P.; Jen-Jacobson, L.; Saxena, S.K.; Sensitive Cu2+-Cu2+ distance measurements in a protein-DNA complex by Double-Quantum Coherence ESR. J. Phys. Chem. B. 2013, 117, 6227-6230.
- Green, U.; Aizenshtat, Z.; Ruthstein, S.; Cohen, H.; Reducing the spin-spin interaction of stable carbon radicals. PCCP, 2013, 15, 6182-6184.
- Green, U.; Aizenshtat, Z.; Ruthstein, S.; Cohen, H.; Stable radicals formation in coals undergoing weathering: effect of coal rank. PCCP, 2012, 14, 13046-13052.
- Ruthstein S.; Stone, K.M.; Cunningham, T.F.; Ming, J.; Cascio, M.; Saxena, S.; Pulsed Electron spin Resonance resolves the coordination site of Cu(II) ions in glycine receptor. Biophysical Journal, 2010, 99(8), 2497-2506.
- Omer L.; Ruthstein S.; Goldfarb, D.; Talmon, Y.; High resolution cryogenic-electron microscopy reveals details of a hexagonal-to-bicontinuous cubic phase transition in mesoporous silica synthesis, J. Am. Chem. Soc., 2009, 131, 12466-12473.
- Ruthstein, S.; Raitsimring, A.M.; Bitton, R.; Frydman, V.; Godt, A.; Goldfarb, D.; Distribution of guest molecules in Pluronic micelles studied by double electron electron spin resonance and small angle X-ray scattering. PCCP, 2009, 11, 148-160.
- Ruthstein, S.; Goldfarb, D.; An EPR tool box for exploring the formation and properties of ordered template mesoporous materials. Electron Paramagnetic Resonance, 2008, 21, 184-215.
- Ruthstein, S.; Goldfarb, D.; Evolution of solution structures during the formation of cubic mesoporous material, KIT-6, determined by double electron electron resonance. J. Phys. Chem. C, 2008, 112, 7102-7109.
- Ruthstein, S.; Schmidt, J.; Kesselman, E.; Popovits-Biro, R.; Frydman, V.; Omer, L.; Talmon, Y.; Goldfarb, D.; Molecular level Processes and nanostructure evolution during the formation of the cubic mesoporous material KIT-6. Chem. Mater. 2008, 20, 2779-2792.
- Ruthstein, S.; Schmidt, J.; Kesselman, E.; Talmon, Y.; Goldfarb, D.; Resolving Intermediate Solution Structure During the Formation of Mesoporous SBA-15. J. Am. Chem. Soc. 2006, 128, 3366-3374.
- Ruthstein, S.; Potapov, A.; Raitsimring, A.M.; Goldfarb, D.; Double Electron Electron Resonance as a Method for Characterization of Micelles. J. Phys. Chem .B. 2005, 109, 22843-22851.
- Ruthstein, S.; Artzi, R.; Goldfarb, D.; Naaman, R.; EPR Studies on the Organization of Self-assembled organic monolayers adsorbed on GaAs. PCCP, 2005, 7, 524-529.
- Ruthstein, S.; Frydman, V.; Goldfarb, D.; Study of the Initial Formation Stages of the Mesoporous Materials SBA-15 Using Spin-Labeled Block Co-polymer Templates. J. Phys. Chem. B. 2004, 108, 9016-9022.
- Ruthstein, S.; Frydman, V.; Kababya, S.; Landau, M.; Goldfarb, D; Study of the Formation of the Mesoporous Material SBA-15 by EPR Spectroscopy. J. Phys. Chem. B. 2003, 107, 1739-1748.
Physical Chemistry II
Introduction to Electron Paramagnetic Resonance Spectroscopy
Physical Chemistry Lab
Protein structure and function, structural biology, magnetic resonance, metalloproteins.
More than 30% of all proteins in the cell exploit one or more metals to perform their specific functions, and over 40% of all enzymes contain metals. Metals are commonly found as natural constituents of proteins; however, many metal ions can be toxic when free in biological fluids. Hence, the human bodies as well as microorganisms have evolved considerable regulatory machinery to acquire, utilize, traffic, detoxify, and otherwise manage the intracellular and extracellular concentrations and types of metal ions. Despite the high regulation of metal ions in the human body, diseases such as Menkes, Wilson, Alzheimer’s, Parkinson’s and Prion’s have been linked with metal binding to proteins.
Dr. Ruthstein’s lab will look into some of the significant and least understood biological processes that are related to metal ion transportation and intracellular distribution, as well as unwanted processes due to high metal concentration or protein mutations. The aims are:
(i) To obtain structural information on intrinsically disordered N-terminal domain in metal transporters (such as Ctr1), in order to understand metal ion transportation to the cells.
(ii) To understand the metal binding mechanism of metal sensors in bacterial cells, in order to shed light on the metal regulatory machinery of the bacteria (CueR, CsoR).
(iii) To explore the copper transport and distribution mechanisms in human cells (from Ctr1 through Atox1 to Atp7b), in order to get to the core of the copper homeostasis mechanism.
(iv) To characterize the role of copper and mutations on the aggregation,folding of proteins, and protein-protein interactions in bacteria and human cells.
To comprehend such processes it is necessary to be sensitive to the structural changes that occur in the protein upon metal binding. The main biophysical tool that is used in the lab of Dr. Ruthstein’s lab is pulsed EPR spectroscopy. The power of EPR lies in the sensitivity to both atomic level changes and nanoscale fluctuations. EPR can characterize properties such as redox state and ligand geometry for different functional states of the protein. In addition, EPR can measure distances between paramagnetic probes up to 80 Å
Ms. Adi Natan