RNDr. Marián Fabián, CSc.



1974 M.Sc. in Biophysics, Charles University, Prague, Czechoslovakia
1981 Ph.D. in Biophysics, Moscow State University, Moscow, USSR


Research Interests:

Main focus of our work is in the understanding of the molecular mechanism of proton pumping by respiratory cytochrome c oxidases. Most intriguing is a chemical nature of two ferryl intermediates produced at the catalytic center during the reaction of CcO with O2. Both intermediates participate in the pumping and it is likely that in one of them the free radical is also present. Our goal is to validate the generation of radical and to establish the protonation state of ferryl intermediates.
Broader area of our interests encompasses the bacterial iron acquisition molecular systems and the structural, functional aspects of heme proteins (microbial flavohemoglobins, myoglobins).



Senior research associate in the Center for Interdisciplinary Biosciences, Faculty of Natural Sciences, Safarik University in Kosice (UPJS)
Specialist in enzymology of the respiratory heme-copper oxidases, heme proteins, the primary reactions in photosynthesis and the bacterial iron acquisition systems


1964 – 67 High school, Handlova, Czechoslovakia
1969 – 74 Charles University, Prague, Czechoslovakia, – MSc. in Biophysics
1977 – 81 Moscow State University, Moscow, USSR – CsC. degree in Biophysics


Slovak, Russian and English

Professional positions:

2013 – present Senior Research Associate at Centre for Interdisciplinary Biosciences, P.J. Šafárik University, Košice, Slovak Republic
1998 – 2013 Faculty and Senior Faculty Fellow, Department of Biochemistry and Cell Biology, Rice University, Houston
1984 – 1991 Head of Biophysical Laboratory, Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Czechoslovakia
1981 – 1984 Head of Biophysical Laboratory, Neurobiological Institute of Slovak Academy of Sciences, Kosice, Czechoslovakia
1974 – 1977 Research Fellow, Neurobiological Institute of Slovak Academy of Sciences, Kosice, Czechoslovakia

Postdoctoral research training:

1991 – 1998 Postdoctoral Research Associate at Department of Biochemistry and Cell Biology, Rice University, Houston with Prof. G. Palmer


Award of Slovak Biophysical Society for the substantial contribution to the development of Biophysics in Slovakia, 2016


2009–2011 NIH grant: Molecular mechanism of redox driven proton pumps Role: Principal Investigator
2002 – 2006 NIH grant: Catalytic Mechanism of Heme-Copper Oxidases Role: Principal Investigator
1998 – 2002 Co-principal investigator in NIH grant: Catalytic Mechanism of Heme-Copper Oxidases
1991 – 1993 Grant from Slovak Academy of Sciences, Czechoslovakia. Role: Principal Investigator
1986 Short term grant from Swedish Academy of Engineering Sciences

Technical expertise:

Experience with variety of spectroscopic methods (optical spectroscopy, electron paramagnetic resonance (EPR), magnetic circular dichroism, Fourier-Transform infrared spectroscopy), fast kinetic methods (stopped flow, laser flash photolysis, rapid-freeze quench method) and methods employed in purification of proteins and computer analysis of data.


49 publications in international peer-reviewed journals (see WOS and Scopus databases), cited more than 1020 times, Hirsch index = 21

Current Projects:

Electron-proton coupling in the respiratory heme-copper oxidases, Slovak Grant Agency (VEGA) 2018-2021.

Number of SCI citation ≈ 1020, Hirsch Index = 21

1. Kopcova, K., Blascakova, L., Kozar, T., Jancura, D. and Fabian, M. Response of Heme Symmetry to the Redox State of Bovine Cytochrome c Oxidase, Biochemistry 57, 4105−4113 (2018).

2. Sjodt. M, Macdonald, R., Spirig, T., Chan, A., Dickson, C. F., Fabian, M., Olson, J. S., Gell. D. A., Clubb, R.T., Clubb, R, T. The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin. J. Mol. Biology 428, 1107-1129 (2016).

3. Jancura, D., Stanicova, J., Palmer, G., Fabian, M. How Hydrogen Peroxide Is Metabolized by Oxidized Cytochrome c Oxidase. Biochemistry 53, 3564−3575 (2014).

4. Liao, Y., Brame, J., Que, W., Xiu, Z., Xie, H., Li, Q., Fabian, M., Alvarez, P. J. Photocatalytic generation of multiple ROS types using low-temperature crystallized anodic TiO2 nanotube arrays. Journal of Hazardous Materials 260, 434– 441 (2013).

5. Musatov, A., Fabian, M. and Varhac, R. Elucidating the mechanism of ferrocytochrome c heme disruption by peroxidized cardiolipin. J Biol Inorg Chem 18, 137–144 (2013).

6. Ekworomadu, M. T., Poor. C. B., Owens, C. P., Balderas, M. A., Fabian, M., Olson, J. S., Murphy, F., Balkabasi, E., Honsa, E. S., He, C., Goulding, C. W., Maresso, A. W. Differential Function of Lip Residues in the Mechanism and Biology of an Anthrax Hemophore. PLoS Pathogens 8, 1-16 (2012).

7. Honsa, E. S., Fabian, M., Cardenas, A. M., Olson, J. S. and Maresso, A. W. The Five Near-iron Transporter (NEAT) Domain Anthrax Hemophore, IsdX2, Scavenges Heme from Hemoglobin and Transfers Heme to the Surface Protein IsdC. J. Biol. Chem. 286, 33652–33660 (2011).

8. Kakar, S., Hoffman, F. G., Storz, J. F., Fabian, M. and Hargrove. M. S. Structure and reactivity of hexacoordinate hemoglobin’s. Biophysical Chemistry, 152, 1-14 (2010).

9. Sedlak, E., Fabian, M., Robinson, N. C. and Musatov, A. Ferricytochrome c protects mitochondrial cytochrome c oxidase against hydrogen peroxide-induced oxidative damage. Free Radical Biology and Medicine 49, 1574-1581 (2010).

10. Tsai, A-l., Berka, V., Martin, F., Ma, X., van den Akker, F., Fabian, M., and Olson, J. S. Is Nostoc HNOX a Gaseous Sensor or a Redox Switch. Biochemistry 49, 6587–6599 6587 (2010).

11. Tarlovsky, Y., Fabian, M., Solomaha, E., Honsa, E., Olson, J. S., and Maresso, A. W. A Bacillus anthracis S-Layer Homology Protein that Binds Heme and Mediates Heme Delivery to IsdC. J. Bacteriology 192, 3503-3511 (2010).Ran, Y., Liu, M., Zhu, H., Nygaard, T. K., Brown, D. E., Fabian, M., Dooley, D. M., and Lei, B. Spectroscopic Identification of Heme Axial Ligands in HtsA That Are Involved in Heme Acquisition by Streptococcus pyogenes. Biochemistry 49, 2834–2842 (2010).

12. Parul, D., Palmer, G., and Fabian, M. Ligand Trapping by Cytochrome c Oxidase: Implications for Gating at the Catalytic Center. J. Biol. Chem. 285, 4536-4543 (2010).

13. Varhac, R., Tomaskova, N., Fabian, M., and Sedlak, E. Kinetics of cyanide binding as a probe of local stability/flexibility of cytochrome c. Biophys. Chem. 144, 21-26, (2009).

14. Fabian, M., Solomaha, E., Olson, J. S., and Maresso, A. Heme Transfer to the Bacterial Cell Envelope Occurs via a Secreted Hemophore in the Gram-positive Pathogen Bacillus anthracis. J. Biol. Chem. 284, 32138-32146 (2009).

15. Zhu, H., Xie, G., Liu, M., Olson, J. S., Fabian, M., Dooley, D. M., and Lei, B. Pathway for heme uptake from human methemoglobin by the iron-regulated surface determinants system of Staphylococcus aureus. J. Biol. Chem. 283, 18450-18460 (2008).

16. Bagelova, J., Fedunova, D., Gazova, Z., Fabian, M., and Antalik, M. Influence of NaCl and sorbitol on the stability of conformations of cytochrome c. Biophys. Chem. 135, 110-115 (2008).

17. Brand, S. E., Rajagukguk, S., Ganesan, K., Geren, L., Fabian, M., Han, D., Gennis, R. B., Durham, B., and Millett, F. A new ruthenium complex to study single-electron reduction of the pulsed OH state of the detergent-solubilized cytochrome oxidase. Biochemistry 46, 14610-14618 (2007).

18. Ran, Y., Zhu, H., Liu, M., Fabian, M., Olson, J. S., Aranda, R., Phillips, Jr., G. N., Dooley, D. M., and Lei, B. Bis-methionine ligation to heme iron in the Streptococcal cell surface protein Shp facilitates rapid hemin transfer to HtsA of the HtsABC transporter. J. Biol. Chem. 282, 31380-31388 (2007).

19. Zhou, S., Olson, J. S., Fabian, M., Weiss, M. J., and Gow, A. J. Biochemical fates of alpha hemoglobin bound to alpha hemoglobin stabilizing protein (AHSP) J. Biol. Chem. 281, 32611-32618 (2006).

20. Nygaard, T. K., Blouin, G. C., Liu, M., Fukumura, M., Olson, J. S., Fabian, M., Dooley, D. M., and Lei, B. The Mechanism of Direct Heme Transfer from the Streptococcal Cell Surface Protein Shp to HtsA of the HtsABC Transporter. J. Biol. Chem. 281, 20761-20771 (2006).

21. Siletsky, S., Han, D., Brand, S., Morgan, J. E., Fabian, M., Geren, L., Millett, F., Durham B., Konstantinov, A. A., and Gennis, R. B. Single-Electron Photoreduction of the PM Intermediate of Cytochrome c Oxidase. Biochim. Biophys. Acta 1757, 1122-1132 (2006).

22. Jancura, D., Berka, V., Antalik, M., Bagelova, J., Gennis, R. G., Palmer, G., and Fabian, M. Spectral and kinetic equivalence of oxidized cytochrome c oxidase as isolated and ‘activated’ by reoxidation. J. Biol. Chem. 281, 30319-30325 (2006).

23. Jancura, D., Antalik, M., Berka, V., Palmer, G., and Fabian, M. Filling the catalytic site of cytochrome c oxidase with electrons: Reduced CuB facilitates internal electron transfer to heme a3. J. Biol. Chem. 281, 20003-20010 (2006).

24. Fabian, M., Jancura, D., Bona, M., Musatov, A., Baran, M., and Palmer, G. The influence of reduction of heme a and CuA on the oxidized catalytic center of cytochrome c oxidase: Insight from organic solvents, Biochemistry 45, 4277-4283 (2006).

25. Antalik, M., Jancura, D., Palmer, G. and Fabian, M. A Role for Protein in Internal Electron Transfer to the Catalytic Center of Cytochrome c Oxidase, Biochemistry 44, 14881-14889 (2005).

26. Parul, D., Palmer, G. and Fabian, M. Proton interactions with hemes a and a3¬ in bovine heart cytochrome c oxidase Biochemistry. 44, 4562-4571 (2005).

27. Fabian, M., Jancura, D., and Palmer, G. Two Sites of Interaction of Anions With Cytochrome a In Oxidized Bovine Cytochrome c Oxidase J. Biol Chem. 279, 16170-16177 (2004).

28. McMahon, B. H., Fabian, M., Tomson, F., Causgrove, T. P., Bailey, J. B., Rein, F. N., R. Dyer, B., Palmer, G., Gennis, R. B., and Woodruff, W. H. FTIR Studies of Internal Proton Transfer Reactions Linked to Inter-heme Electron Transfer in Bovine Cytochrome c Oxidase, Biochim. Biophys. Acta 1655, 321-331 (2004).

29. Fabian, M., Skultety,, L., Jancura, D. and Palmer, G. Implications of Ligand Binding Studies for the Catalytic Mechanism of Cytochrome c Oxidase Biochim. Biophys. Acta 1655, 298-305 (2004).

30. Fabian, M., Skultety, L., Brunel, C., and Palmer, G., The cyanide stimulated dissociation of chloride from the catalytic center of oxidized oxidase, Biochemistry 40, 6061–6069 (2001).

31. Fabian, M., and Palmer, G., Proton involvement in the transition of “peroxy” to “ferryl” intermediate of cytochrome c oxidase, Biochemistry 40, 1867-1874 (2001).

32. Fabian, M., Wong, W.W., Gennis, R.B., and Palmer, G., Mass spectrometric determination of dioxygen bond splitting in the “peroxy” form of cytochrome c oxidase, Proc. Natl. Acad. Sci. USA 96, 13114-13117 (1999).

33. Fabian, M., and Palmer, G., The redox state of peroxy and ferryl intermediates in cytochrome c oxidase catalysis, Biochemistry 38, 6270-6275 (1999).

34. Fabian, M., and Palmer, G., Hydrogen peroxide is not released following reaction of cyanide with several catalytically important derivatives of cytochrome c oxidase, FEBS Lett. 422, 1-4 (1998).

35. Wallace-Williams, S.E., James, C.E., de Vries, S., Saraste, M., Lappalainen, P., van der Ost, J., Fabian, M., Palmer, G., and Woodruff, W.H., Far-red resonance Raman study of Copper A in subunit II of cytochrome c oxidase, J. Am. Chem. Soc. 118, 3986-3987 (1996).

36. Fabian, M., and Palmer, G., The interaction of cytochrome oxidase with hydrogen peroxide: The relationship of compounds P and F, Biochemistry 34, 13802-13810 (1995).

37. Fabian, M., and Palmer, G., The reaction of cyanide with peroxidatic forms of cytochrome oxidase, Biochemistry 34, 1534-1540 (1995).

38. Berka, V., Tikhonov, A.A., Svarcberger, J., and Fabian, M., Dependence of spectral and structural properties of resting cytochrome oxidase on temperature, Biochemistry Inter. 28, 277-286 (1992).

39. Musatov, A., Fabian, M., and Dadak, V., Mitochondrial cytochrome c oxidase: Structure and function, Biology 46, 1113-1125 (1991).

40. Bona, M., Fabian, M., and Sedlak, M., Spectral and catalytic properties of cytochrome oxidase in organic solvents, Biochim. Biophys. Acta 1020, 94-100 (1990).

41. Fabian, M., and Malmström, B.G., The effect of pH changes on the optical spectrum of oxidised cytochrome oxidase, Biochim. Biophys. Acta 973, 414-419 (1989).

42. Fabian, M., and Jalcova, H., The effect of freezing and thawing on the spectral properties of cytochrome oxidase, Biology 43, 701-707 (1988).

43. Fabian, M., and Jalcova, H., The effect of freezing and thawing on the spectral properties of cytochrome oxidase, Biology 43, 701-707 (1988).

44. Zakharova, N.I., Fabian, M., Kononenko, A.A., Chamarovskij, S.K., Luksene, Z.B., and Rubin, A.B., Temperature dependence of protein globule polarization and electron transfer in photosynthetic reaction centers from Rhodopseudomonas sphaeroides, Molecular Biology (Engl. Trans.) 19, 562-568 (1985).

45. Zakharova, N.I., Fabian, M., Uspenskaja, N.J., Kononenko, A.A., and Rubin, A.B., Structural and functional characteristics of photosynthetic reaction centers isolated from R. sphaeroides, Biochemistry (Engl. Trans.) 46, 1351-1357 (1982).

46. Fabian, M., Chamarovskij, S.K., Zakharova, N.I., Selivanov, V.A., Kononenko, A.A., and Rubin, A.B., Light induced pH changes and buffering capacity of the suspension of photosynthetic reaction centers from R. sphaeroides, Molecular Biology (Engl. Trans.) 15, 351-357 (1981).

47. Fabian, M., Zakharova, N.I., Chamarovskij, S.K., and Kononenko, A.A., Effect of pH on the photo induced electron transfer in Rhodopseudomonas sphaeroides reaction centers, Molecular Biology (Engl. Trans.) 14, 944-948 (1981).


In the field of respiratory cytochrome c oxidases our studies contributed to:
– the contemporary understanding of the nature of the catalytic ferryl intermediates [see Publications 3, 21, 31-34, 36, 37, 47]
– the identification of the control mechanisms of internal electron transfer [23, 25, 28]
– the uncovering the functionally important intramolecular interactions [1, 24, 26, 27, 29, 30, 41]
– the nature of reoxidized ‘macroergic’ state of CcO [22]
In the field of bacterial iron acquisition systems:
– to the determination of the sequence of the interprotein heme transfer in ABC transmembrane transporters [2, 4, 6-8].