Springe direkt zu Inhalt

Dr. Jacek Kozuch

Kozuch

Fachbereich Physik

Institut für experimentelle Physik

Experimentelle Molekulare Biophysik

Adresse
Arnimallee 14
Raum 1.1.35
14195 Berlin
Homepage

Electrostatic Effects in Biological Processes

I aim at understanding how electrostatic interactions sculpt structural motifs in biological macromolecules and give rise to their unrivalled functionalities. In particular, I am interested in such structures found in enzymatic active sites, ion/proton channel pores as well as complex assemblies within biological membranes.

I explore this question with a particular focus on the mechanisms of evolution towards antimicrobial resistances, which present a major global health issue of today’s world. As such, I have studied the evolution of electrostatic catalysis in antibiotic resistance against β-lactam antibiotics previously. Now, I am extending this concept to the interplay between electrostatic and protonation effects, for instance, in the proton conductance through viral proton channels as part of the Collaborative Research Center 1078 (https://www.sfb1078.de/). Towards this goal I use a multidisciplinary experimental and theoretical approach centered around advanced vibrational spectroscopic approaches.

Preprinted Publications

24. C. Zheng, Y. Mao, J. Kozuch, A. Atsango, Z. Ji, T. Markland, S. G. Boxer, Electric field orientations in solution and enzyme active site revealed by a two-dimensional vibrational probe, ChemRxiv, 2021.
https://doi.org/10.33774/chemrxiv-2021-578vg

23. S. H. Schneider, J. Kozuch, S. G. Boxer, The interplay of electrostatics and chemical positioning in the evolution of antibiotic resistance in TEM beta-lactamases, bioRxiv, 2021.

https://doi.org/10.1101/2021.05.27.446023

Peer-Reviewed Publications

22. J. Kozuch, S. H. Schneider, C. Zheng, Z. Ji, R. T. Bradshaw, S. G. Boxer, Testing the limitations of MD-based local electric fields using the vibrational Stark effect in solution: pencillin G as a test case, J. Phys. Chem. B, 2021, 125, 4415-4427.
https://doi.org/10.1021/acs.jpcb.1c00578

21. F. Baserga, J. Drageli, J. Kozuch, H. Mohrmann, E.-W. Knapp. S. T. Stripp, J. Heberle, Quantification of local electric field changes in the active site of cytochrome c oxidase by FTIR spectroelectrochemical titrations, Front. Chem., 2021, 9, 669452.
https://doi.org/10.3389/fchem.2021.669452

20. J. Kozuch, S. H. Schneider, S. G. Boxer Biosynthetic incorporation of site-specific isotopes in β-lactam antibiotics enables biophysical studies, ACS Chem. Bio., 2020, 15, 1148-1153.
https://doi.org/10.1021/acschembio.9b01054

19. U. Szczepaniak, S. H. Schneider, R. Horvath, J. Kozuch, M. Geiser Vibrational Stark spectroscopy of fluorobenzene using quantum cascade laser dual frequency combs, Appl. Spec., 2020, 74, 347-356.
https://doi.org/10.1177/0003702819888503

18. A. de Miguel Catalina, E. Forbrig, J. Kozuch, C. Nehls, L. Paulowski, T. Gutsmann, P. Hildebrandt, M. A. Mroginski The C-terminal VPRTES tail of LL-37 influences the mode of attachment to a lipid bilayer and antimicrobial activity, Biochemistry, 2019, 58, 2447-2464.
https://doi.org/10.1021/acs.biochem.8b01297

17. M. Caterino, M. Herrmann, A. Merlino, C. Ricciardi, D. Montesarchio, M. A. Mroginski, D. Musumeci, F. Ruffo, L. Paduano, P. Hildebrandt, J. Kozuch, A. Vergara On the pH-modulated Ru-based pro-drug activation mechanism, Inorg. Chem., 2018, 58, 1216-1223.
https://doi.org/10.1021/acs.inorgchem.8b02667

16. H. Biava, T. Schreiber, S. Katz, J.-S. Völler, M. Stolarski, C. Schulz, N. Michael, N. Budisa, J. Kozuch, T. Utesch, P. Hildebrandt Long-range modulations of the electric fields in proteins, J. Phys. Chem. B, 2018, 122, 8330-8342.
https://doi.org/10.1021/acs.jpcb.8b03870

15. T. G. G. A. Harris, N. Heidary, J. Kozuch, S. Frielingsdorf, O. Lenz, M. A. Mroginski, P. Hildebrandt, I. Zebger, A. Fischer, In situ spectroelectrochemical studies into the formation and stability of robust diazoniumderived interfaces on gold electrodes for the immobilization of an oxygen-tolerant hydrogenase, ACS Appl. Mater. Interfaces, 2018, 10, 23380-23391.
https://doi.org/10.1021/acsami.8b02273

14. O. Gutierrez-Sanz, E. Forbrig, A. P. Batista, M. I. Pereira, J. Salewski, M. A. Mroginski, R. Götz, A. L. De Lacey, J. Kozuch, I. Zebger, Catalytic activity and proton translocation of reconstituted respiratory complex I monitored by surface-enhanced infrared absorption spectroscopy, Langmuir, 2018, 34, 57023-5711.
https://doi.org/10.1021/acs.langmuir.7b04057

13. P. Kielb, M. Horch, P. Wrzolek, R. Götz, H. K. Ly, J. Kozuch, M. Schwalbe, I. Weidinger, Hydrogen Evolution by cobalt hangman porphyrins under operating conditions studied by vibrational spectro-electrochemistry, Catal. Sci. Technol., 2018, 8, 1849-1857.
https://doi.org/10.1039/C7CY02253K

12. E. Forbrig, J. K. Staffa, J. Salewski, M. A. Mroginski, P. Hildebrandt, J. Kozuch, Monitoring the orientational changes of alamethicin during incorporation in bilayer lipid membranes, Langmuir, 2018, 34, 2373-2385.
https://doi.org/10.1021/acs.langmuir.7b04265

11. J. K. Staffa, L. Lorenz, M. Stolarski, D. H. Murgida, I. Zebger, T. Utesch, J. Kozuch, P. Hildebrandt, Determination of the local electric field at Au/SAM interfaces using the vibrational Stark effect, J. Phys. Chem. C, 2017, 121, 22274-22285.
https://doi.org/10.1021/acs.jpcc.7b08434

10. P. Kielb, T. Utesch, J. Kozuch, J.-H. Jeoung, H. Dobbek, M. A. Mroginski, P. Hildebrandt, I. Weidinger, Switchable redox chemistry of the hexameric tyrosine-coordinated heme protein, J. Phys. Chem. B, 2017, 121, 3955-3964.
https://doi.org/10.1021/acs.jpcb.7b01286

9. S. Wiebalck, J. Kozuch, C. C. Tzschucke, L. J. C. Jeuken, P. Hildebrandt, Monitoring the transmembrane proton gradient generated by cytochrome bo3 in tethered bilayer lipid membranes using SEIRA spectroscopy, J. Phys. Chem. B, 2016, 120, 22492256.
https://doi.org/10.1021/acs.jpcb.6b01435

8. H. K. Ly, P. Wrzolek, N. Heidary, R. Götz, M. Horch, J. Kozuch, M. Schwalbe, I. Weidinger, 2nd coordination sphere controlled electron transfer of iron hangman complexes on rlectrodes probed by surface-enhanced vibrational spectroscopy, Chem. Sci., 2015, 6, 6999-7007.
https://doi.org/10.1039/C5SC02560E

7. J. Kozuch, N. Petrusch, D. Gkogkou, U. Gernert, I. M. Weidinger, Calculating average surface-enhancement factors of randomly nanostructured electrodes by a combination of SERS and impedance Spectroscopy, Phys. Chem. Chem. Phys., 2015, 17, 21220-21225.
https://doi.org/10.1039/C4CP05015K

6. J. Kozuch, C. Weichbrodt, D. Millo, K. Giller, S. Becker, P. Hildebrandt, C. Steinem, Voltage-dependent structural changes of the membrane-bound anion channel hVDAC1 probed by SEIRA and electrochemical impedance spectroscopy, Phys. Chem. Chem. Phys., 2014, 16, 9546-9555.
https://doi.org/10.1039/C4CP00167B

5. X. X. Han, C. Köhler, J. Kozuch, U. Kuhlmann, L. Paasche, A. Sivanesan, I. M. Weidinger, P. Hildebrandt, Potential-Dependent surface-enhanced resonance Raman spectroscopy at nanostructured TiO2: a case study on cytochrome b5, Small, 2013, 9, 4175-4181.
https://doi.org/10.1002/smll.201301070

4. J. Kozuch, I. von der Hocht, F. Hilbers, H. Michel, I. M. Weidinger, Resonance Raman Characterization of the ammonia-generated intermediate of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry, 2013, 52, 6197-6202.
https://doi.org/10.1021/bi400535m

3. J. Kozuch, C. Steinem, P. Hildebrandt, D. Millo, Combined electrochemistry and surface-enhanced infrared absorption spectroscopy of gramicidin A incorporated into tethered bilayer lipid membranes. Angew. Chem. Int. Ed., 2012, 51, 8114-8117.
https://doi.org/10.1002/anie.201203214

2. A. Sivanesan, J. Kozuch, H. K. Ly, G. Kalaivani, A. Fischer, I. M. Weidinger, Tailored silica coated Ag nanoparticles for non-invasive surface enhanced Raman spectroscopy of biomolecular targets, RSC Adv., 2012, 2, 805-808.
https://doi.org/10.1039/C1RA00781E

1. A. Sivanesan, H. K. Ly, J. Kozuch, M. Sezer, U. Kuhlmann, A. Fischer, I. M. Weidinger, Functionalized Ag nanoparticles with tunable optical properties for selective protein analysis, Chem. Commun., 2011, 47, 3553-3555.
https://doi.org/10.1039/C0CC05058J