Veterinärmedizinische Universität Wien
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Kurzbeschreibung
The Electron Spin Resonance (ESR) spectrometer, or Electron Paramagnetic Resonance (EPR) spectrometer, is an instrument to study (bio-)molecules, which have one or more unpaired electrons, such as free radicals (including reactive oxygen and nitrogen species) and complexes of transition metals. The EMX ESR spectrometer has an X-band microwave bridge and is used for the detection of radicals and paramagnetic transition metals in biomimetic and biological model systems, such as buffers, cell cultures, subcellular fractions, blood, plasma and tissue pieces.
Ansprechperson
Ao. Prof. Dr. Lars Gille
Research Services
The ESR spectrometer can be used by internal and external scientists in cooperation with local ESR experts.
Methoden & Expertise zur Forschungsinfrastruktur
Besides the importance of the ESR technique for non-biological subjects, several radical species were detected in living organisms, such as oxygen radicals or the endothelium-derived relaxing factor (EDRF, NO), which are of significant biological importance. Furthermore, this technique is relevant in biophysical research for the study of lipid membrane properties of cells and organelles as well as the binding of labeled molecules, such as drugs, to cellular structures. For the application of ESR spectroscopy in biological systems several specialized techniques were developed.
The ESR spectroscopy was already employed in our lab for following applications:
- Detection of oxygen radicals in biological model systems (1)
- Detection of vitamin c radicals and NO (EDRF) in blood and plasma(2)
- Evaluation of antioxidants (3)
- Measurement of membrane fluidity of lipid memranes (4)
- Elucidation of chemical reaction mechanisms (5)
References:
1. A. Haschemi, P. Kosma, L. Gille, C. R. Evans, C. F. Burant, P. Starkl, B. Knapp, R. Haas, J. A. Schmid, C. Jandl, S. Amir, G. Lubec, J. Park, H. Esterbauer, M. Bilban, L. Brizuela, J. A. Pospisilik, L. E. Otterbein, and O. Wagner. The sedoheptulose kinase CARKL directs macrophage polarization through control of glucose metabolism. Cell Metab. 15 (6):813-826, 2012.
2. L. Gille, M. Kleiter, M. Willmann, and H. Nohl. Paramagnetic species in the plasma of dogs with lymphoma prior to and after treatment with doxorubicin. An ESR study. Biochem.Pharmacol. 64 (12):1737-1744, 2002.
3. H. Nohl, L. Gille, and A. V. Kozlov. Antioxidant-derived prooxidant formation from ubiquinol. Free Radic.Biol.Med. 25 (6):666-675, 1998.
4. E. A. Malingriaux, A. Ruprecht, L. Gille, O. Jovanovic, P. Jezek, M. Jaburek, and E. E. Pohl. Fatty acids are key in 4-hydroxy-2-nonenal-mediated activation of uncoupling proteins 1 and 2. Plos One 8 (10):e77786, 2013.
5. C. R. Kowol, P. Heffeter, W. Miklos, L. Gille, R. Trondl, L. Cappellacci, W. Berger, and B. K. Keppler. Mechanisms underlying reductant-induced reactive oxygen species formation by anticancer copper(II) compounds. J.Biol.Inorg.Chem. 17 (3):409-423, 2012.
ausgefüllt werden
Department of Parasitology, Institute of Tropical Medicine “Pedro Kourí”, Havana, Cuba
Department of Pharmacology, Institute of Postgradual Medical Education & Research, Kolkata, India
Institute of Physiology, Pathophysiology and Biophysics, University of Veterinary Medicine, Vienna, Austria
Institute of Inorganic Chemistry, University of Vienna, Vienna, Austria
Institute of Cancer Research and Comprehensive Cancer Center, Medical University of Vienna, Vienna, Austria
Chemistry Department, University of Potsdam, Golm/Potsdam, Germany
A. Haschemi, P. Kosma, L. Gille, C. R. Evans, C. F. Burant, P. Starkl, B. Knapp, R. Haas, J. A. Schmid, C. Jandl, S. Amir, G. Lubec, J. Park, H. Esterbauer, M. Bilban, L. Brizuela, J. A. Pospisilik, L. E. Otterbein, and O. Wagner. The sedoheptulose kinase CARKL directs macrophage polarization through control of glucose metabolism. Cell Metab. 15 (6):813-826, 2012.
L. Gille, M. Kleiter, M. Willmann, and H. Nohl. Paramagnetic species in the plasma of dogs with lymphoma prior to and after treatment with doxorubicin. An ESR study. Biochem.Pharmacol. 64 (12):1737-1744, 2002.
H. Nohl, L. Gille, and A. V. Kozlov. Antioxidant-derived prooxidant formation from ubiquinol. Free Radic.Biol.Med. 25 (6):666-675, 1998.
E. A. Malingriaux, A. Ruprecht, L. Gille, O. Jovanovic, P. Jezek, M. Jaburek, and E. E. Pohl. Fatty acids are key in 4-hydroxy-2-nonenal-mediated activation of uncoupling proteins 1 and 2. Plos One 8 (10):e77786, 2013.
C. R. Kowol, P. Heffeter, W. Miklos, L. Gille, R. Trondl, L. Cappellacci, W. Berger, and B. K. Keppler. Mechanisms underlying reductant-induced reactive oxygen species formation by anticancer copper(II) compounds. J.Biol.Inorg.Chem. 17 (3):409-423, 2012.