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Biography
Prof. Alexander A. Konstantinov

Prof. Alexander A. Konstantinov

Moscow State University, Russia


Email: konst@genebee.msu.su


Qualifications


1985 Ph.D., Biochemistry, Moscow State University

1972 M.Sc., Biochemistry, Moscow State University


Publications (selected)

  1. Vos, M.H., Borisov,V.B., Liebl,U., Martin,J.L., Konstantinov,A.A. (2000) Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: a di-heme active site? Proc. Natl. Acad. Sci. USA 97, 1554-1559.
  2. Jasaitis, A., Borisov, V. B., Belevich, N. P., Morgan, J. E., Konstantinov, A. A., and Verkhovsky, M. I. (2000) Electrogenic reactions of cytochrome bd. Biochemistry. 39:13800-13809.
  3. Dzhagarov. B.M., Belyanovich, L.M., Konstantinov,A.A., Rudenok,A.A. and Tikhomirov, S.A. (2000) Picosecond absorption spectroscopy of cytochrome c oxidase: excited states and relaxation processes in the heme groups of cytochromes a and a3. Dokl. Akad. Nauk 375, 112-114
  4. Borisov, V. N., Selednikova, S. E., Poole, R. E., and Konstantinov, A. A. (2001) Interaction of cytochrome bd with carbon monoxide at low and room temperatures. J.Biol.Chem. 276, 22095-22099
  5. Pecoraro, C., Gennis R. B., Vygodina, T. V., and Konstantinov, A. A. (2001) Role of the K-channel in the pH-dependence of the Reaction of Cytochrome c Oxidase with Hydrogen Peroxide. Biochemistry 40, 9695-9708
  6. Zhang, J., Hellwig, P., Osborne, J. P., Huang, H.-w., Moenne-Loccoz, P., Konstantinov, A. A., and Gennis, R. B. (2001) Site-directed mutations of the highly conserved region near the Q-loop of the cytochrome bd quinol oxidase from Escherichia coli specifically perturbs heme b595. Biochemistry 40, 8548-8556
  7. Borisov,V.B., Liebl,U., Rappaport,F., Martin, J.-L., Zhang,J., Gennis, R., Konstantinov, A.A. and Vos, M. (2002) Interactions between Heme d and Heme b595 in Quinol Oxidase bd from Escherichia coli: A Photoselection Study Using Femtosecond Spectroscopy. Biochemistry 41, 1654-1662
  8. Azarkina, N, Konstantinov, A.A. (2002) Stimulation of menaquinone-dependent electron transfer in the respiratory chain of Bacillus subtilis by membrane energization. Journal Bacteriology 184, 5339-47.
  9. Lee, A, Kirichenko, A, Vygodina, T, Siletsky, S.A, Das, T.K, Rousseau, D.L, Gennis, R, Konstantinov AA. (2002) Ca(2+)-binding site in Rhodobacter sphaeroides cytochrome C oxidase. Biochemistry 41, 8886-98.
  10. Pereverzev, M.O, Vygodina, T.V, Konstantinov, A.A, Skulachev, V.P. (2003) Cytochrome c, an ideal antioxidant. Biochem. Soc. Transac. 31, 1312-5. Review.
  11. Borisov, V.B, Forte, E, Konstantinov, A.A, Poole, R.K, Sarti, P, Giuffrè, A. (2004) Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide. FEBS Lett. 576, 201-4.
  12. Siletsky, S.A, Pawate, A.S, Weiss, K, Gennis, R.B, Konstantinov, A.A. (2004) Transmembrane charge separation during the ferryl-oxo -> oxidized transition in a nonpumping mutant of cytochrome c oxidase. J. Biol. Chem. 279, 52558-65.
  13. Kirichenko, A.V, Pfitzner, U, Ludwig, B, Soares, C.M, Vygodina, T.V, Konstantinov, A.A. (2005) Cytochrome c oxidase as a calcium binding protein. Studies on the role of a conserved aspartate in helices XI-XII cytoplasmic loop in cation binding. Biochemistry. 44, 12391-401.
  14. Belevich I, Borisov VB, Konstantinov AA, Verkhovsky MI. (2005) Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability. FEBS Lett. 579,4567-70.
  15. Kuznetsova, S.S, Azarkina, N.V, Vygodina, T.V, Siletsky, S.A, Konstantinov, A.A. (2005) Zinc ions as cytochrome C oxidase inhibitors: two sites of action. Biochemistry (Mosc). 70, 128-36.
  16. Fernandes, A.S, Konstantinov, A.A, Teixeira, M, Pereira, M.M. (2005) Quinone reduction by Rhodothermus marinus succinate:menaquinone oxidoreductase is not stimulated by the membrane potential. Biochem. Biophys. Res. Commun. 330, 565-70.
  17. Belevich, I, Borisov, V.B, Zhang, J, Yang, K, Konstantinov, A.A, Gennis, R.B, Verkhovsky, M.I. (2005) Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site. Proc. Natl Acad Sci. U S A 102, 3657-62.
  18. Siletsky, S.A, Han, D, Brand, S, Morgan, J.E, Fabian, M, Geren, L, Millett, F, Durham, B, Konstantinov, A.A, Gennis, R.B. (2006) Single-electron photoreduction of the P(M) intermediate of cytochrome c oxidase. Biochimica Biophysica Acta. 1757,1122-32.
  19. Borisov, V.B, Forte, E, Sarti, P, Brunori, M, Konstantinov, A.A, Giuffrè, A. (2006) Nitric oxide reacts with the ferryl-oxo catalytic intermediate of the CuB-lacking cytochrome bd terminal oxidase. FEBS Lett. 580, 4823-6.
  20. Vygodina TV, Konstantinov AA. (2007) Peroxidase activity of mitochondrial cytochrome с oxidase. Biochemistry (Mosc) 72, 1056-64.
  21. Siletsky, S.A, Belevich, I, Jasaitis, A, Konstantinov, A.A, Wikström, M, Soulimane, T, Verkhovsky, M.I. (2007) Time-resolved single-turnover of ba(3) oxidase from Thermus thermophilus. Biochim. Biophys. Acta 1767, 1383-92.
  22. Belevich, I, Borisov, V.B, Bloch, D.A, Konstantinov, A.A, Verkhovsky, M.I. (2007) Cytochrome bd from Azotobacter vinelandii: evidence for high-affinity oxygen binding. Biochemistry 46, 11177-84.
  23. Borisov, V.B, Forte, E, Sarti, P, Brunori, M, Konstantinov, A.A, Giuffrè, A.(2007) Redox control of fast ligand dissociation from Escherichia coli cytochrome bd. Biochem. Biophys. Res. Commun. 355, 97-102.
  24. Forte, E., Borisov, V.B., Konstantinov, A.A., Brunori, M., Giuffrè, A., Sarti, P. (2007) Cytochrome bd, a key oxidase in bacterial survival and tolerance to nitrosative stress.Ital J Biochem.56, 265-269.
  25. Arutyunyan. A.M, Borisov, V.B., Novoderezhkin, V.I., Ghaim, J., Zhang, J., Gennis, R.B., Konstantinov, A.A. (2008) Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: the Fe-to-Fe distance between hemes d and b595 is 10 A. Biochemistry 47, 1752-1759
  26. Yang, K., Borisov, V.B., Konstantinov, A.A., Gennis, R.B. (2008) The fully oxidized form of the cytochrome bd quinol oxidase from E. coli does not participate in the catalytic cycle: direct evidence from rapid kinetics studies.FEBS Lett. 582, 3705-3709

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