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Publikacje

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  1. Borek A., Wójcik-Augustyn A., Kuleta P., Ekiert R., Osyczka A. (2023) Identification of hydrogen bonding network for proton transfer at the quinol oxidation site of Rhodobacter capsulatus cytochrome bc1. J. Biol. Chem. 299(10): 105249

  2. Welc-Stanowska R., Pietras R., Mielecki B., Sarewicz M., Luchowski R., Widomska J., Grudziński W., Osyczka A., Gruszecki W. I. (2023) How Do Xanthophylls Protect Lipid Membranes from Oxidative Damage? J. Phys. Chem. Lett. 14: 7440-7444
  3. Kuleta P., Pietras R., Andrys-Olek J., Wójcik-Augustyn A., Osyczka A. (2023) Probing molecular interactions of semiquinone radicals at quinone reduction sites of cytochrome bc1 by X-band HYSCORE EPR spectroscopy and quantum mechanical calculations, Phys. Chem. Chem Psych., 25: 21935
  4. Sarewicz M., Szwalec M., Pintscher S., Indyka P., Rawski M., Pietras R., Mielecki B., Koziej Ł., Jaciuk M., Glatt S., Osyczka A. (2023) High-resolution cryo-EM structures of plant cytochrome b6f at work, Science Advances, 9: eadd968
  5. Bujnowicz Ł., Pietras R., Sarewicz M., Osyczka A. (2023) Low-cost stopped-flow and freeze-quench device for double mixing, Hardware X, 14: e00409
  6. Borek A., Ekiert R., Osyczka A. (2023), On the inter-monomer electron transfer in cytochrome bc1, BBA - Bioenergetics, 1864: 148981

  1.  Kozioł J., Froncisz W. (2022) Functioning of EPR Automatic Frequency Control in the Presence of the Circulator’s Spurious Leakage, Applied Magnetic Resonance volume 53:  207–220
  2. Bujnowicz Ł., Sarewicz M. (2022) Multichannel pulse high-current driver of magnetic actuator, HardwareX, 11: 00286
  3. Szwalec M., Bujnowicz Ł., Sarewicz M., Osyczka A. (2022) Unexpected Heme Redox Potential Values Implicate an Uphill Step in Cytochrome b6f, J. Phys. Chem. B, 47: 9771–9780
  4. Kania A., Bratek M., Majta J., Sarapata K., Gałan W., Markiewicz M., Wójcik-Augustyn A. (2022) The importance of atomic partail charges in the reproduction of intermolecular interactions for the triacetin - a model of glycerol backbone, Chemistry and Physics of Lipids, 245: 105203

 

  1. Sarewicz M., Osyczka A. (2021). Cytochrome bc1 complex (respiratory chain complex III). In: Encyclopedia of Biological Chemistry III (Jez, J. Ed.) Eslevier INC. col. 2: 502-511
  2. Kuleta P., Lasham J., Sarewicz M., Ekiert I., Sharma V., Ekiert R., Osyczka A (2021) Hydrogen bonding rearrangement by a mitochondrial disease mutation in cytochrome bc1 perturbs heme bH redox potential and spin state. Proc. Nat. Acad. Sci. USA 118, e2026169118
  3. Lorencik K., Ekiert R., Zhu Y., McBride M. J., Gennis R. B., Sarewicz M., Osyczka A. (2021). Monoheme c Subunit of Respiratory Alternative Complex III Is Not Essential for Electron Transfer to Cytochrome aa3 in Flavobacterium johnsoniae. Microbiol Spectr. 9: e0013521.
  4. Sarewicz M., Pintscher S., Bujnowicz Ł., Wolska M., Osyczka A. (2021). The High-Spin Heme bL Mutant Exposes Dominant Reaction Leading to the Formation of the Semiquinone Spin-Coupled to the [2Fe-2S]+ Cluster at the Qo Site of Rhodobacter capsulatus Cytochrome bc1. Front. Chem. 9:658877
  5. Sarewicz M., Pintscher S., Pietras R., Borek A., Bujnowicz Ł., Hanke G., Cramer W. A., Finazzi G., Osyczka A., (2021). Catalytic Reactions and Energy Conservation in the Cytochrome bc1 and b6f Complexes of Energy-Transducing Membranes, Chemical Reviews 121: 2020-2108
  6. Kozioł J., Rajda P., Rumian R., Oleś T., Budzioch P., Gurbiel R. J., Froncisz W. (2021). Continuous wave electron paramagnetic resonance L-band spectrometer with direct digitalization using time-locked subsampling. Journal of Magnetic Resonance 322: 106870
  7. Pagacz J., Broniec A., Wolska M., Osyczka A., Borek A. (2021). ROS signaling capacity of cytochrome bc1: Opposing effects of adaptive and pathogenic mitochondrial mutations, Free Radical Biology and Medicine 163: 243-254

 

  1. Pintscher, S., Wójcik-Augustyn, A., Sarewicz, M., Osyczka, A. (2020). Charge polarization imposed by the binding site facilitates enzymatic redox reactions of quinone. BBA-Bioenergetics 1861: 148216
  2. Bujnowicz Ł., Sarewicz M., Osyczka A. (2020) Nietypowy semichinon jako element buforujący przepływ elektronów przez cytochromy z rodziny bc, Postępy Biochemii 66: 91 – 99
  3. Purhonen J, Grigorjev V, Ekiert R, Aho N, Rajendran J, Pietras R, Truvé K, Wikström M, Sharma V, Osyczka A, Fellman V, Kallijärvi J. (2020). A spontaneous mitonuclear epistasis converging on Rieske Fe-S protein exacerbates complex III deficiency in mice. Nature Communications  11: 322

  1. Bujnowicz Ł., Borek A., Kuleta P., Sarewicz M., Osyczka A. (2019). Suppression of superoxide production by a spin-spin coupling between semiquinone and the Rieske cluster in cytochrome bc1. FEBS Lett. 593, 3-12
  2. Godlewska U., Bilska B., Zegar A., Brzoza P., Borek A., Murzyn K., Bocheńska O., Morytko A., Kuleta P., Kozik A., Pyza E., Osyczka A., Zabel B. A., Cichy J. (2019). The antimicrobial activity of chemerin-derived peptide p4 requires oxidative conditions. J Biol Chem, 2019 vol. 294 no. 4, p. 1267-1278

  1. 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. 593, 3-12
  2. 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
  3. Pintscher S, Pietras R, Sarewicz M, Osyczka A, (2018) Electron sweep across four b-hemes of cytochrome bc1 revealed by unusual paramagnetic properties of the Qi semiquinone intermediate Bioch. Biophys. Acta 1859, 459-469
  4. Sarewicz, M. Bujnowicz, Ł., Osyczka, A. (2018) Generation of semiquinone-[2Fe-2S]+ spin-coupled center at the Qo site of cytochrome bc1 in redox-poised, illuminated photosynthetic chromatopchores from Rhodobacter capsulatus Bioch. Biophys. Acta 1859, 145-153
  5. 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.
  6. Dutka M., Pyka J., Płonka P.M. (2019) EPR Studies on Understanding the Physical Intricacy of HbNO Complexes. In: Shukla A. (eds) Electron Spin Resonance Spectroscopy in Medicine: 23-43.

  1. Bhaduri, S., Stadnytskyi, V., Zakharov, S.D., Hasan, S.S., Bujnowicz, Ł., Sarewicz, M., Savikhin, S., Osyczka, A., Cramer, W.A., (2017) Pathways of transmembrane electron transfer in cytochrome bc complexes: dielectric heterogeneity and interheme coulombic interactions J. Phys. Chem. B 121, 975-983
  2. Sarewicz, M., Bujnowicz, Ł., Bhaduri, S., Singh, S.K., Cramer, W.A., Osyczka, A. (2017) Metastable radical state, nonreactive with oxygen, is inherent to catalysis by respiratory and photosynthetic cytochromes bc1/b6f Proc. Nat. Acad. Sci. USA 114, 1323-1328

  1. Postila, P.A., Kaszuba, K., Kuleta, P., Vattulainen, I., Sarewicz, M., Osyczka, A., Róg, T. (2016) Atomistic determinants of co-enzyme Q reduction at the Qi-site of the cytochrome bc1 complex Sci. Rep. 6, 33607
  2. Kuleta, P., Sarewicz, M., Postila, P., Róg, T., Osyczka, A. (2016) Identifying involvement of Lys251/Asp252 pair in electron transfer and associated proton transfer at the quinone reduction site of Rhodobacter capsulatus cytochrome bc1 BBA Bioenergetics 1857, 10, 1661-1668
  3. 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
  4. Piertras, R., Sarewicz, M., Osyczka, A. (2016) Distinct properties of semiquinone species detected at the ubiquinol oxidation Qo site of cytochrome bc1 and their mechanistic implications J. R. Soc. Interface 13 (118)
  5. Sarewicz, M., Ekiert, R., Osyczka A. (2016) Book chapter: Inter-Monomer Electron Transfer in Cytochrome bc Complexes in: Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling Advances in Photosynthesis and Respiration vol. 41 (Springer)
  6. 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
  7. Pintscher, S., Kuleta, P., Cieluch, E., Sarewicz, M., Osyczka, A. (2016) Tuning of hemes b equilibrium redox potential is not required for cross-membrane electron transfer. J Biol Chem 291, 6872-6881 

  1. 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
  2. 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
  3. Sarewicz, M., Osyczka, A. (2015) Electronic Connection Between the Quinone and Cytochrome c Redox Pools and Its Role in Regulation of Mitochondrial Electron Transport and Redox Signaling. Physiol Rev. 95:219-243

  1. Pietras, R., Sarewicz, M., Osyczka, A. (2014) Molecular organization of cytochrome c2 near the binding domain of cytochrome bc1 studied by electron spin-lattice relaxation enhancement. J Phys Chem B 118: 6634–6643
  2. Ekiert, R., Czapla, M., Sarewicz, M., Osyczka, A. (2014) Hybrid fusions show that inner-monomer electron transfer robustly supports cytochrome bc1 function in vivo. Biochem Biophys Res Commun 451: 270–275

  1. Sarewicz, M., Dutka, M., Pintscher, S., Osyczka, A. (2013) Triplet State of the Semiquinone-Rieske Cluster as an Intermediate of Electronic Bifurcation Catalyzed by Cytochrome bc1. Biochemistry 52 (37), 6388–6395
  2. Pöyry, S., Cramariuc, O., Postila, P.A., Kaszuba, K., Sarewicz, M., Osyczka, A., Vattulainen, I., Róg, T.(2013)Atomistic simulations indicate cardiolipin to have an integral role in the structure of the cytochrome bc1 complex. Biochim Biophys Acta 1827(6):769-78
  3. Postila, P.A., Kaszuba, K., Sarewicz, M., Osyczka, A., Vattulainen, I., Róg, T.(2013)Key role of water in proton transfer at the Qo-site of the cytochrome bc1 complex predicted by atomistic molecular dynamics simulations. Biochim Biophys Acta 1827(6):761-8
  4. 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
  5. Kaszuba, K., Postila, P.A., Cramariuc, O., Sarewicz, M., Osyczka, A., Vattulainen, I., Róg, T. (2013) Parameterization of the prosthetic redox centers of the bacterial cytochrome bc 1 complex for atomistic molecular dynamics simulations Theor Chem Acc 132:1370

  1. Czapla, M., Sarewicz, M., and Osyczka, A. (2012) Fusing proteins as an approach to study bioenergetic enzymes and processes. Biochim Biophys Acta. 1817(10), 1847-1851
  2. Rutheford, A. W., Osyczka, A., and Rappaport, F. (2012) Back-reactions, short circuits, leaks and other energy wasteful reactions in biological electron transfer: Redox tuning to survive life in O2. FEBS Lett. 586, 603-616
  3. 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
  4. 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

  1. Sarewicz, M., Pietras, R., Froncisz, W., and Osyczka, A. (2011) Reorientation of cytochrome c2 upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer. Metallomics 3, 404-409.

  1. 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
  2. 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
  3. Cieluch, E., Pietryga K., Sarewicz, M., Osyczka, A. (2010) Visualizing changes in electron distribution in coupled chains of cytochrome bc1 by modifying barrier for electron transfer between the FeS cluster and heme c1, BBA Bioenergetics, 1797, 296-303
  4. Sarewicz, M., Dutka, M., Froncisz, W., Osyczka, A. (2009) Magnetic Interactions Sense Changes in Distance between Heme bL and the Iron−Sulfur Cluster in Cytochrome bc1, Biochemistry 48, 5708-5720
  5. Zhang, H., Chobot, S. E., Osyczka, A., Wraight, C. A., Dutton, P. L., and Moser, C. C. (2008) Quinone and non-quinone redox couples in complex III. J. Bioenerg. Biomembr. 40, 493-499.  
  6. 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
  7. 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
  8. Sarewicz, M., Szytuła, S., Dutka, M., Osyczka, A., Froncisz, W. (2008) Estimation of binding parameters for the protein-protein interaction using a site-directed spin labeling and EPR spectroscopy, Eur Biophys J 34, 483-493