Svistunenko, Dima - University of Essex - School of Biological Sciences

个人简介

2008-present Director, Biomedical EPR Facility, Department of Biological Sciences, University of Essex 1995-2008 Research Officer, Department of Biological Sciences, University of Essex 1994-1995 Visiting staff, Department of Biological Sciences, University of Essex 1984-1994 Research Associate, Institute of Chemical Physics, Russian Academy of Sciences, Moscow

研究领域

My research interests are centred on proteins and enzymes with particular reference to their paramagnetism. A molecule is called “paramagnetic” if it has an odd number of electrons. Usually, electrons in molecules come in pairs, so an even number of electrons in most chemical structures is typical. But for many biologically important molecules involved in redox reactions, there must exist states which are one electron more or one electron less than the stable even number of electrons state. These molecular states of odd number of electrons (the paramagnetic states!) are chemically active and are major players in proteins and enzymes mechanisms. Thus we study these states of enzymes and proteins to understand how they work and to elucidate their role in normal metabolism and in some abnormalities (diseases).

近期论文

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Cooper, C. E., Schaer, D. J., Buehler, P. W., Wilson, M.T., Reeder, B. J., Silkstone, G., Svistunenko, D. A., Bulow, L., and Alayash, A. I. (2012) Haptoglobin bindng stabilizes hemoglobin ferryl iron and the globin radical on tyrosine b145. Antioxid. Redox Signal (in press). Reeder, B., Svistunenko, D., Cooper, C., and Wilson, M. (2012) Engineering tyrosine-based electron flow pathways in proteins: the case of Aplysia myoglobin. J. Am. Chem. Soc. 134 (18) 7741-7749 Svistunenko, D. A., Worrall, J. A. R., Chugh, S. B., Haigh, S. C., Ghiladi, R.A., and Nicholls, P. (2012) Ferric haem forms of Mycobacterium tuberculosis catalase-peroxidase probed by EPR spectroscopy: their stability and interplay with pH. Biochimie, 94 (6), 1274-1280 Svistunenko, D. A., Adelusi, M., Dawson, M., Robinson, P., Bernini, C., Sinicropi, A., and Basosi, R. (2011) Computation informed selection of parameters for protein radical EPR spectra simulation. Studia UBB Chemia, 56 (3), 135 – 146 Reeder, B. J., Svistunenko, D. A., and Wilson, M. T. (2011) Lipid binding to cytoglobin leads to a change in haem co-ordination: a role for cytoglobin in lipid signalling of oxidative stress, Biochem. J., 434, 483-492 Thompson, M. K., Franzen, S., Ghiladi, R. A., Reeder, B. J., and Svistunenko, D. A. (2010) Compound ES of dehaloperoxidase decays via two alternative pathways depending on the conformation of the distal histidine, J. Am. Chem. Soc., 132 (49): 17501-17510 Demidchik, V., Cuin, T.A., Svistunenko, D., Smith, S.J., Miller, A. J., Shabala, S., Sokolik, A., and Yurin, V. (2010) Arabidopsis root K+ efflux conductance activated by hydroxyl radicals: single-channel properties, genetic basis and involvement in stress-induced cell death. J. Cell Sci. 123, Issue 9, 1468-1479 Mot, A., Zoltan, K., Svistunenko, D. A., Damian, G, Silaghi-Dumitrescu, R., and Makarov, S. V. (2010) ‘Super-reduced’ iron under physiologically-relevant conditions . Dalton Trans., 39, Issue 6, 1464 - 1466 Svistunenko, D.A., and Jones, G.A. (2009) Tyrosyl radicals in proteins: a comparison of empirical and density functional calculated EPR parameters. Phys. Chem. Chem. Phys., 11, 6600-6613 Reeder, B. J., Grey, M., Silaghi-Dumitrescu, R. L., Svistunenko, D. A., Bulow, L., Cooper, C. E., and Wilson, M. T. (2008) Tyrosine residues as redox cofactors in human hemoglobin: Implications for engineering non toxic blood substitutes. J. Biol. Chem., 283, 45, 30780-30787 Chauhan, N., Basran, J., Efimov, I., Svistunenko, D. A., Seward, H. E., Moody, P. C. and Raven, E. L. (2008) The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase. Biochemistry, 47, 16, 4761-4769