prof. dr hab. Artur Osyczka

Profesor nadzwyczajny
Senior Research Fellow of the Wellcome Trust  

 

 

2014 Profesor nauk biologicznych 
2007 Habilitacja (Biofizyka); Uniwersytet Jagielloński
1999 Dr (Biologia ); Tokyo Metropolitan University
1993 Mgr (Biologia; Biochemia); Uniwersytet Jagielloński

Pokój: A027
tel.: 12 664 63 48
e-mail: artur.osyczka(at)uj.edu.pl

 

Staże naukowe:

1999-2006 Po-doktorancke w laboratorium P. Leslie Dutton, University of Pennsylvania, Department of Biochemistry and Molecular Biophysics
1996-1999 Doktoranckie w laboratorium Katsumi Matsuura, Tokyo Metropolitan University, Department of Biology
1994 University of California in Los Angeles
1992 University of Wales in Bangor

 

Dorobek naukowy:

  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

  3. 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

  4. 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

  5. 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

  6. 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)

  7. 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)

  8. 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

  9. 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 

  10. 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

  11. 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 29023781-23792

  12. 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

  13. 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

  14. 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

  15. 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

  16. 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

  17. 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

  18. 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

  19. 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

  20. 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

  21. Rutherford, 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

  22. Czapla. M., Borek, A., Sarewicz, M., and Osyczka, A. (2012) Enzymatic activities of isolated cytochrome bc1-like complexes containing fused cytochrome b subunits with asymmetrically inactivated segments of electron transfer chains. Biochemistry 51, 829-835.

  23. 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.

  24. 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.

  25. Sarewicz, M., Borek, A., Cieluch, E., Świerczek, M., and Osyczka, A. (2010) Discrimination between two possible reaction sequences that create potential risk of generation of deleterious radicals by cytochrome bc1. Implications for the mechanism of superoxide production. Biochim. Biophys. Acta 1797, 1820-1827.

  26. Świerczek, M., Cieluch, E., Sarewicz, M., Borek, A., Moser, C. C., Dutton, P. L., and Osyczka, A. (2010) An electronic bus bar lies in the core of cytochrome bc1. Science 329, 451-454.

  27. Cieluch, E., Pietryga, K., Sarewicz, M., and 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. Biochim. Biophys. Acta 1797, 296-303.

  28. Sarewicz, M., Dutka, M., Froncisz, W., and Osyczka, A. (2009) Magnetic interactions sense changes in distance between heme bL and the iron-sulfur cluster in cytochrome bc1. Biochemistry 48, 5708-5720.

  29. 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.

  30. Borek, A., Sarewicz, M., and 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.

  31. Sarewicz, M., Borek, A., Daldal, F., Froncisz, W., and Osyczka, A. (2008) Demonstration of short-lived complexes of cytochrome c with cytochrome bc1 by EPR spectroscopy. Implications for the mechanism of interprotein electron transfer. J. Biol. Chem. 283, 14826-24836.

  32. Lee, D-W., Ozturk, Y., Osyczka, A., Cooley, J. W., and Daldal, F. (2008) Cytochrome bc1-cy fusion complexes reveal the distance constraints for functional electron transfer between photosynthetic components. J. Biol. Chem. 283, 13973-13982.

  33. Ozturk, Y., Lee, D-W., Mandaci, S., Osyczka, A., Prince, R. C., and Daldal, F. (2008) Soluble variants of Rhodobacter capsulatus membrane-anchored cytochrome cy are efficient photosynthetic electron carriers. J. Biol. Chem. 283, 13964-13972.

  34. Sarewicz, M., Szytuła, S., Dutka, M., Osyczka, A., and Froncisz, W. (2008) Estimation of binding parameters for the protein-protein interaction using a site-directed spin labeling and EPR spectroscopy. Eur. Biophys. J. 37, 483-493.

  35. Zhang, H., Osyczka, A., Dutton, P. L., and Moser, C. C. (2007) Exposing the complex III Qo site semiquinone radical. Biochim. Biophys. Acta 1767, 883-887.

  36. Zhang, H., Osyczka, A., Moser, C. C., and Dutton, P. L. (2006) Resilience of Rhodobacter sphaeroides cytochrome bc1 to heme c1 ligation changes. Biochemistry 45, 14247-14255.

  37. Osyczka, A., Zhang, H., Mathe, C., Rich, P. R., Moser, C. C., and Dutton, P. L. (2006) Role of the PEWY glutamate in hydroquinone-quinone oxidation-reduction catalysis in the Qo site of cytochrome bc1. Biochemistry 45, 10492-10503.

  38. Lee, D-W., Oztruk, Y., Mamedova, A., Osyczka, A., Cooley, J. W., and Daldal, F. (2006) A functional hybrid between the cytochrome bc1 complex and its physiological membrane anchored electron acceptor cytochrome cy in Rhodobacter capsulatus. Biochim. Biophys. Acta 1757, 346-352.

  39. Moser, C. C., Osyczka, A., and Dutton, P. L. (2005) Short-circuit proofing Mitchell's Q cycle, in: "Photosynthesis: Fundamental Aspects to Global Perspectives", (Bruce, D., and van der Est A., ed.) Allen Press, 427-430.

  40. Nanda, V., Rosenblatt, M. M., Osyczka, A., Kono, H., Getahun, Z., Dutton, P. L., Saven, J. G., and DeGrado, W. F. (2005) De novo design of a redox active minimal rubredoxin mimic. J. Am. Chem. Soc. 127, 5804-5805.

  41. Osyczka A., Moser C. C., and Dutton P. L. (2005) Fixing the Q cycle. Trends Bioch. Sci. 30, 176-182.

  42. Iwaki, M., Yakovlev, G., Hirst, J., Osyczka, A., Dutton, P. L., Marshall, D., and Rich, P. R. (2005) Direct observation of redox-linked histidine protonation changes in the iron-sulfur protein of cytochrome bc1 complex by ATR-FTIR spectroscopy. Biochemistry 44, 4230-4237.

  43. Iwaki, M., Osyczka, A., Moser, C. C., Dutton, P. L., and Rich, P. R. (2004) ATR-FTIR spectroscopy studies of iron-sulfur protein and cytochrome c1 in Rhodobacter capsulatus cytochrome bc1. Biochemistry 43, 9477-9486.

  44. Ghirlanda, G., Osyczka, A., Liu, W., Antolovich, M., Smith, K. M., Dutton, P. L., Wand, A. J., and DeGrado, W. F. (2004) De novo design of a D2-symmetrical protein that reproduces the di-heme 4-helix bundle in cytochrome bc1. J. Am. Chem. Soc. 126, 8141-8147.

  45. Osyczka, A., Moser, C. C., Daldal, F., and Dutton, P. L. (2004) Reversible redox energy coupling in electron transfer chains. Nature 427, 607-612.

  46. Osyczka, A., Moser, C. C., and Dutton, P. L. (2004) Novel cyanide inhibition at cytochrome c1 of Rhodobacter capsulatus cytochrome bc1. Biochim. Biophys. Acta 1655, 71-76.

  47. Li, J., Osyczka, A., Conover, R. C., Johnson, M. K., Qin, H., Daldal, F., and Knaff, D. B. (2003) The role of acidic and aromatic amino acids in Rhodobacter capsulatus cytochrome c1. A site-directed mutagenesis study. Biochemistry 42, 8818-8830.

  48. Li, J., Darrouzet, E., Dhawan, I. K., Johnson, M. K., Osyczka, A., Daldal, F., and Knaff, D. B. (2002) Spectroscopic and oxidation-reduction properties of Rhodobacter capsulatus cytochrome c1 and its M183K and M183H variants. Biochim. Biophys. Acta, 1556, 175-186.

  49. Osyczka, A., Dutton, P. L., Moser, C. C., Darrouzet, E., and Daldal, F. (2001) Controlling the functionality of cytochrome c1 redox potentials in Rhodobacter capsulatus bc1 complex through disulfide anchoring of a loop and a β-branched amino acid near the heme-ligating methionine. Biochemistry 40, 14547-14556.

  50. Pyka, J., Osyczka, A., Turyna, B., Blicharski, W., and Froncisz, W. (2001) EPR studies of iso-1-cytochrome c: effect of temperature on two-component spectra of spin label attached to cysteine at position 102 and 47. Eur. Biophys. J. 30, 367-373.

  51. Osyczka, A., Nagashima, K. V. P., Sogabe, S., Miki, K., Shimada, K., and Matsuura, K. (2001) Different mechanisms of the binding of soluble electron donors to the photosynthetic reaction center of Rubrivivax gelatinosus and Blastochloris viridis. J. Biol. Chem. 276, 24108-24112.

  52. Pyka, J., Osyczka, A., Turyna, B., Blicharski, W., and Froncisz, W. (1999) Probing iso-1-cytochrome c structure by site-directed spin labeling and electron paramagnetic resonance techniques. Acta Biochimica Polonica 46, 889-899.

  53. Osyczka, A., Nagashima, K. V. P., Sogabe, S., Miki, K., Shimada, K., and Matsuura, K. (1999) Comparison of the binding sites for high-potential iron-sulfur protein and cytochrome c on the tetraheme cytochrome subunit bound to the bacterial photosynthetic reaction center. Biochemistry 38, 15779-15790.

  54. Osyczka, A., Nagashima, K. V. P., Shimada, K., and Matsuura, K. (1999) Interaction site for high-potential iron-sulfur protein on the tetraheme cytochrome subunit bound to the photosynthetic reaction center of Rubrivivax gelatinosus. Biochemistry 38, 2861-2865.

  55. Osyczka, A., Nagashima, K. V. P., Sogabe, S., Miki, K., Yoshida, M., Shimada, K., and Matsuura, K. (1998) Docking site for soluble electron carriers on the tetraheme cytochrome subunit bound to the bacterial photosynthetic reaction center, in: "Photosynthesis: Mechanisms and Effects" (Garab, G. ed.), vol. II, Kluwer Academic Publishers, Dordrecht, 901-904.

  56. Osyczka, A., Nagashima, K. V. P., Sogabe, S., Miki, K., Yoshida, M., Shimada, K., and Matsuura, K. (1998) Interaction site for soluble cytochromes on the tetraheme cytochrome subunit bound to the bacterial reaction center mapped by site-directed mutagenesis. Biochemistry 37, 11732-11744.

  57. Turyna, B., Osyczka, A., Kostrzewa, A., Blicharski, W., Enghild, J. J., and Froncisz, W. (1998) Preparation and electron paramagnetic resonance characterization of spin labeled monoderivatives of horse cytochrome c. Biochim. Biophys. Acta 1386, 50-58.

  58. Osyczka, A., Yoshida, M., Nagashima, K. V. P., Shimada, K., and Matsuura, K. (1997) Electron transfer from high-potential iron-sulfur protein and low-potential cytochrome c-551 to the primary donor of Rubrivivax gelatinosus reaction center mutationally devoid of the bound cytochrome subunit. Biochim. Biophys. Acta 1321, 93-99.

  59. Hilczer, W., Goslar, J., Gramza, M., Hoffmann, S. K., Blicharski, W., Osyczka, A., Turyna, B., and Froncisz, W. (1995) A resonance enhancement of the phase relaxation in the electron spin echo of nitroxide covalently attached to cytochrome c. Chem. Phys. Lett. 247, 601-606.

  60. Osyczka, A., and Turyna, B. (1995) Cytochrome c conformations and its interactions with cytochrome c oxidase. Advances in Biochemistry 41, 59-66.

  61. Osyczka, A., and Turyna, B. (1994) Site-specific incorporation of unnatural amino acids into proteins. Advances in Cell Biology 21, 175-185.