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Prof. Ludmila A. Golovleva

Russian Academy of Sciences, Russia


Email: Golovleva@ibpm.pushchino.ruLudmila-golovleva@rambler.ru



1980 Doctor of Sciences, USSR Academy of Sciences, Biology, Institute of Biochemistry and Physiology of microorganisms

1966 Ph.D., M.V. Lomonosov Moscow State University, Chemical Faculty, Organic chemistry

1962 M.Sc., M.V. Lomonosov Moscow State University, Biological Faculty, Microbiology


Publications (Selected)

  1. Fujiwara M., Golovleva L.A., Saeki Y., Nozaki M., Hayaishi O. Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad. J Biol Chem, 1975, 250(13):4848-55.
  2. Bruschi M., Hatchikian C.E., Golovleva L.A., Gall J.L., Purification and characterization of cytochrome c3, ferredoxin, and rubredoxin isolated from Desulfovibrio desulfuricans Norway. J Bacteriol, 1977, 129(1):30-8.
  3. Kataeva I.A., Golovleva L.A., Catechol 2, 3-dioxygenases from Pseudomonas aeruginosa 2x. Methods Enzymol, 1990, 188:115-21.
  4. Golovleva L.A., Pertsova R.N., Boronin A.M., Travkin V.M., Kozlovsky S.A., Kelthane degradation by genetically engineered Pseudomonas aeruginosa BS827 in a soil ecosystem. Appl Environ Microbiol., 1988, 54(6):1587-1590.
  5. Maltseva O.V., Niku-Paavola M.L., Leontievsky A.A., Myasoedova N.M., Golovleva L.A., Ligninolytic enzymes of the white rot fungus Panus tigrinus. Biotechnology and applied biochemistry, 1991, 13:291-302.
  6. Golovleva LA, Zaborina O, Pertsova R, Baskunov B, Schurukhin Y, Kuzmin S., Degradation of polychlorinated phenols by Streptomyces rochei 303. Biodegradation, 1991-1992, 2(3):201-208.
  7. Maltseva O.V., Solyanikova I.P., Golovleva L.A., Chlorocatechol 1,2-dioxygenase from Rhodococcus erythropolis 1CP. Kinetic and immunochemical comparison with analogous enzymes from gram-negative strains. Eur J Biochem., 1994, 226(3):1053-61.
  8. Pozdnyakova N., Leontievsky A., Golovleva L., Oxidase of the white rot fungus Panus tigrinus 8/18. FEBS Lett., 1994, 350(2-3):192-194.
  9. Leontievsky A., Myasoedova N., Pozdnyakova N., Golovleva L., 'Yellow' laccase of Panus tigrinus oxidizes non-phenolic substrates without electron-transfer mediators. FEBS Lett., 1997, 413(3):446-448.
  10. Travkin V.M., Jadan A.P., Briganti F., Scozzafava A., Golovleva L.A., Characterization of an intradiol dioxygenase involved in the biodegradation of the chlorophenoxy herbicides 2,4-D and 2,4,5-T. FEBS Lett., 1997, 407(1):69-72.
  11. Rodakiewicz-Nowak J., Haber J., Pozdnyakova N., Leontievsky A., Golovleva L.A., Effect of ethanol on enzymatic activity of fungal laccases. Biosci Rep., 1999, 19(6):589-600.
  12. Leontievsky A.A., Myasoedova N.M., Baskunov B.P., Evans C.S., Golovleva L.A., Transformation of 2,4,6-trichlorophenol by the white rot fungi Panus tigrinus and Coriolus versicolor. Biodegradation, 2000, 11(5):331-40.
  13. Moiseeva O.V., Solyanikova I.P., Kaschabek S.R., Gröning J., Thiel M., Golovleva L.A., Schlömann M. A new modified ortho cleavage pathway of 3-chlorocatechol degradation by Rhodococcus opacus 1CP: genetic and biochemical evidence. J Bacteriol., 2002, 184(19):5282-92.
  14. Travkin V., Baskunov B.P., Golovlev E.L., Boersma M.G., Boeren S., Vervoort J., van Berkel W.J., Rietjens I.M., Golovleva L.A., Reductive deamination as a new step in the anaerobic microbial degradation of halogenated anilines. FEMS Microbiol Lett., 2002, 209(2):307-12.
  15. Solyanikova I.P., Moiseeva O.V., Boeren S., Boersma M.G., Kolomytseva M.P., Vervoort J., Rietjens I.M., Golovleva L.A., van Berkel W.J., Conversion of 2-fluoromuconate to cis-dienelactone by purified enzymes of Rhodococcus opacus 1cp. Appl Environ Microbiol., 2003, 69(9):5636-42.
  16. Zaborina O., Latus M., Eberspächer J., Golovleva L.A., Lingens F., Purification and characterization of 6-chlorohydroxyquinol 1,2-dioxygenase from Streptomyces rochei 303: comparison with an analogous enzyme from Azotobacter sp. strain GP1. J Bacteriol., 1995, 177(1):229-34.
  17. Solyanikova I.P., Maltseva O.V., Vollmer M.D., Golovleva L.A., Schlömann M., Characterization of muconate and chloromuconate cycloisomerase from Rhodococcus erythropolis 1CP: indications for functionally convergent evolution among bacterial cycloisomerases. J Bacteriol., 1995, 177(10):2821-2826.
  18. Eulberg D., Golovleva L.A., Schlömann M., Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP. J Bacteriol., 1997, 179(2):370-81.
  19. Leontievsky A.A., Vares T., Lankinen P., Shergill J.K., Pozdnyakova N.N., Myasoedova N.M., Kalkkinen N., Golovleva L.A., Cammack R., Thurston C.F., Hatakka A., Blue and yellow laccases of ligninolytic fungi. FEMS Microbiol Lett., 1997, 156(1):9-14.
  20. Eulberg D., Lakner S., Golovleva L.A., Schlömann M., Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity. J Bacteriol., 1998, 180(5):1072-1081.
  21. Eulberg D., Kourbatova E.M., Golovleva L.A., Schlömann M., Evolutionary relationship between chlorocatechol catabolic enzymes from Rhodococcus opacus 1CP and their counterparts in proteobacteria: sequence divergence and functional convergence. J Bacteriol., 1998, 180(5):1082-1094.
  22. Moiseeva O.V., Solyanikova I.P., Kaschabek S.R., Gröning J., Thiel M., Golovleva L.A., Schlömann M., A new modified ortho- cleavage pathway of 3-chlorocatechol degradation by Rhodococcus opacus 1CP: genetic and biochemical evidence. J Bacteriol., 2002, 184(19):5282-5292.
  23. Lisov A.V., Leontievsky A.A., Golovleva L.A., Hybrid Mn-peroxidases of Bazidiomycetes. Appl. Biochem.Microbiol., 2007, 43(5):598-606.
  24. Ferraroni M.,Myasoedova N., Schmatchenko V., Leontievsky A., Golovleva L., Scozzafava A., Briganti F., Crystal structure of a blue laccase from Panus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases. BMC Structural Biology, 2007, 7:60.
  25. Kolomytseva M., Baskunov B ., Golovleva L., Intradiol pathway of para-cresol conversion by Rhodococcus opacus 1 cp. Biotechnology Journal, 2007, 2:886-893.