Arkadiusz Borek, PhD
Research Assistant
2015 PhD (Biophysics); Jagiellonian University
2007 MSc (Biotechnology; Biophysics); Jagiellonian University
Contact
room: A024
phone: 12 664 64 21
e-mail: arkadiusz.borek(at)uj.edu.pl
Scholarships
2014-2017 Stypendium Ministra dla wybitnych młodych naukowców.
2016 Nagroda Rektora zespołowa II stopnia za osiągnięcia naukowe.
2011 Stypendium START
2010 Nagroda zespołowa Rektora UJ za publikację w czasopiśmie Science.
Work experience
from 2005 Department of Molecular Biophysics, Jagiellonian University
2006 intership in Medical College of Wisconsin, Milwaukee, USA
Publications:
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Bujnowicz Ł., Borek A., Kuleta P., Osyczka A., (2018) Suppression of superoxide production by a spin-spin coupling between semiquinone and Rieske cluster. FEBS Lett. in press
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Borek A, Ekiert R., Osyczka A, (2018) Functional flexibility of electron flow between quinol oxidation Qo site of cytochrome bc1 and cytochrome c revealed by combinatory effects of mutations in cytochrome b, iron-sulfur protein and cytochrome c1 Bioch. Biophys. Acta 1859, 754-761
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Borek A, Ekiert R, Osyczka A, (2018) Advances in understanding mechanism and physiology of cytochromes bc. Book chapter in: Mechanisms of primary energy transduction in biology. Chemical biology no. 5. Edited by M. Wikström. Royal Society of Chemistry London pp. 192-214.
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Borek, A., Ekiert, R., Osyczka, A. (2016) Molekularne efekty mutacji mitochondrialnych w genie kodującym cytochrom b kompleksu III i ich wpływ na poziom produkcji wolnych rodników Postępy Biochemii 62 (2) 162-172
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Ekiert, E., Borek, A., Kuleta, P., Czernek, J., Osyczka, A. (2016) Mitochondrial disease-related mutations at the cytochrome b-iron-sulfur protein (ISP) interface: Molecular effects on the large-scale motion of ISP and superoxide generation studied in Rhodobacter capsulatus cytochrome bc1. BBA Bioenergetics
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Sarewicz, M., Dutka, M., Pietras, R., Borek, A., Osyczka, A. (2015) Effect of H bond removal and changes in the position of the iron-sulphur head domain on the spin-lattice relaxation properties of the [2Fe-2S](2+) Rieske cluster in cytochrome bc(1). Phys Chem Chem Phys 17(38), 25297-25308
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Borek, A., Kuleta, P., Ekiert, R., Pietras, R., Sarewicz, M., Osyczka, A. (2015) Mitochondrial Disease-related Mutation G167P in Cytochrome b of Rhodobacter capsulatus Cytochrome bc1 (S151P in Human) Affects the Equilibrium Distribution of [2Fe-2S] Cluster and Generation of Superoxide. J Biol Chem 290, 23781-23792
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Czapla, M., Cieluch, E., Borek, A., Sarewicz, M., Osyczka, A.(2013)Catalytically-relevant electron transfer between two hemes bL in the hybrid cytochrome bc1-like complex containing a fusion of Rhodobacter sphaeroides and capsulatus cytochromes b. Biochim Biophys Acta 1827(6):751-60
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Czapla, M., Borek, A., Sarewicz, M., and Osyczka, A., (2012) Enzymatic activities of isolated cytochrome bc1-like complexes containing fused cytochromoe b subunits with asymmetrically inactivated segments of electron transfer chains. Biochemistry 51, 829-835
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Czapla, M., Borek, A., Sarewicz, M., and Osyczka, A., (2012) Fusing two cytochromes b of Rhodobacter capsulatus cytochrome bc1 using various linkers defines a set of protein templates for asymmetric mutagenesis. Protein Eng., Des. Sel. 25, 15-25
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Sarewicz, M., Borek, A., Cieluch, E., Świerczek, M., Osyczka A. (2010) Discrimination between to possible reaction sequences that create potential risk of generation of deleterious radicals by cytochrome bc1: implications for the mechanism of superoxide production. BBA Bioenergetics, 1797, 1820-1827
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Świerczek, M., Cieluch, E., Sarewicz, M., Borek, A., Moser, C.C., Dutton, P. L., Osyczka, A. (2010). An electronic bus bar lies in the core of cytochrome bc1. Science, 329, 451-454
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Borek, A., Sarewicz, M., Osyczka, A. (2008) Movement of the Iron−Sulfur Head Domain of Cytochrome bc1 Transiently Opens the Catalytic Qo Site for Reaction with Oxygen, Biochemistry 47, 12365-12370
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Sarewicz, M., Borek, A., Daldal, F., Froncisz, W., Osyczka, A. (2008) Demonstration of Short-lived Complexes of Cytochrome c with Cytochrome bc1 by EPR Spectroscopy, J Biol Chem 283, 24826-24836