Education

Docent, University of Helsinki, Finland, 2000

Current position

docent, Institute of Biotechnology, University of Helsinki, Finland

Publications

1. Belevich, N., Belevich, G., Chen, Z., Sinha, S. C. and Verkhovskaya, M. (2017). Activation of respiratory Complex I from Escherichia coli studied by fluorescent probes. Heliyon 3(1): e00224.
2. Belevich, N. and Verkhovskaya, M. (2016). Resting state of respiratory Complex I from Escherichia coli. FEBS Lett 590(11): 1570-1575.
3. Bogachev, A. V., Bertsova, Y. V., Verkhovskaya, M. L., Mamedov, M. D. and Skulachev, V. P. (2016). Real-time kinetics of electrogenic Na(+) transport by rhodopsin from the marine flavobacterium Dokdonia sp. PRO95. Sci Rep 6: 21397.
4. Belevich, N. P., Bertsova, Y. V., Verkhovskaya, M. L., Baykov, A. A. and Bogachev, A. V. (2016). Identification of the coupling step in Na(+)-translocating NADH:quinone oxidoreductase from real-time kinetics of electron transfer. Biochim Biophys Acta 1857(2): 141-149.
5. Sharma, V., Belevich, G., Gamiz-Hernandez, A. P., Rog, T., Vattulainen, I., Verkhovskaya, M. L., Wikstrom, M., Hummer, G. and Kaila, V. R. (2015). Redox-induced activation of the proton pump in the respiratory complex I. Proc Natl Acad Sci U S A 112(37): 11571-11576.
6. Belevich, N., Belevich, G. and Verkhovskaya, M. (2014). Real-time optical studies of respiratory Complex I turnover. Biochim Biophys Acta 1837(12): 1973-1980.
7. Knuuti, J., Belevich, G., Sharma, V., Bloch, D. A. and Verkhovskaya, M. (2013). A single amino acid residue controls ROS production in the respiratory Complex I from Escherichia coli. Mol Microbiol 90(6): 1190-1200.
8. Verkhovskaya, M. and Bloch, D. A. (2013). Energy-converting respiratory Complex I: on the way to the molecular mechanism of the proton pump. Int J Biochem Cell Biol 45(2): 491-511.
9. Verkhovsky, M., Bloch, D. A. and Verkhovskaya, M. (2012). Tightly-bound ubiquinone in the Escherichia coli respiratory complex I. Biochim Biophys Acta 1817(9): 1550-1556.
10. Belevich, G., Knuuti, J., Verkhovsky, M. I., Wikstrom, M. and Verkhovskaya, M. (2011). Probing the mechanistic role of the long alpha-helix in subunit L of respiratory Complex I from Escherichia coli by site-directed mutagenesis. Mol Microbiol 82(5): 1086-1095.
11. Verkhovskaya, M., Knuuti, J. and Wikstrom, M. (2011). Role of Ca(2+) in structure and function of Complex I from Escherichia coli. Biochim Biophys Acta 1807(1): 36-41.
12. Borisov, V. B., Murali, R., Verkhovskaya, M. L., Bloch, D. A., Han, H., Gennis, R. B. and Verkhovsky, M. I. (2011). Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc Natl Acad Sci U S A 108(42): 17320-17324.
13. Verkhovskaya, M., Knuuti, J. and Wikstrom, M. (2011). Role of Ca(2+) in structure and function of Complex I from Escherichia coli. Biochim Biophys Acta 1807(1): 36-41.
14. Belevich, N. P., Verkhovskaya, M. L. and Verkhovsky, M. I. (2009). Chapter 4 Electron transfer in respiratory complexes resolved by an ultra-fast freeze-quench approach. Methods Enzymol 456: 75-93.
15. Euro, L., Belevich, G., Wikstrom, M. and Verkhovskaya, M. (2009). High affinity cation-binding sites in Complex I from Escherichia coli. Biochim Biophys Acta 1787(8): 1024-1028.
16. Euro, L., Bloch, D. A., Wikstrom, M., Verkhovsky, M. I. and Verkhovskaya, M. (2008). Electrostatic interactions between FeS clusters in NADH:ubiquinone oxidoreductase (Complex I) from Escherichia coli. Biochemistry 47(10): 3185-3193.
17. Euro, L., Belevich, G., Verkhovsky, M. I., Wikstrom, M. and Verkhovskaya, M. (2008). Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I). Biochim Biophys Acta 1777(9): 1166-1172.
18. Verkhovskaya, M. L., Belevich, N., Euro, L., Wikstrom, M. and Verkhovsky, M. I. (2008). Real-time electron transfer in respiratory complex I. Proc Natl Acad Sci U S A 105(10): 3763-3767.
19. Belevich, G., Euro, L., Wikstrom, M. and Verkhovskaya, M. (2007). Role of the conserved arginine 274 and histidine 224 and 228 residues in the NuoCD subunit of complex I from Escherichia coli. Biochemistry 46(2): 526-533. 
20. Sinegina, L., Wikstrom, M., Verkhovsky, M. I. and Verkhovskaya, M. L. (2005). Activation of isolated NADH:ubiquinone reductase I (complex I) from Escherichia coli by detergent and phospholipids. Recovery of ubiquinone reductase activity and changes in EPR signals of iron-sulfur clusters. Biochemistry 44(23): 8500-8506.
21. Verkhovskaya, M. L., Barquera, B. and Wikstrom, M. (2001). Deletion of one of two Escherichia coli genes encoding putative Na+/H+ exchangers (ycgO) perturbs cytoplasmic alkali cation balance at low osmolarity. Microbiology 147(Pt 11): 3005-3013.
22. Gomes, C. M., Backgren, C., Teixeira, M., Puustinen, A., Verkhovskaya, M. L., Wikstrom, M. and Verkhovsky, M. I. (2001). Heme-copper oxidases with modified D- and K-pathways are yet efficient proton pumps. FEBS Lett 497(2-3): 159-164.
23. Pereira, M. M., Verkhovskaya, M. L., Teixeira, M. and Verkhovsky, M. I. (2000). The caa(3) terminal oxidase of Rhodothermus marinus lacking the key glutamate of the D-channel is a proton pump. Biochemistry 39(21): 6336-6340.