Vladimir O. Popov


 

popov_new-копия_small Vladimir O. Popov
Professor, Dr.Sci (Chemistry), Corresponding Member of the Russian Academy of Sciences
Director of the Research Centre of Biotechnology RAS
Head of Laboratory of Enzyme Engineering
Телефон +7 (495) 952-34-41
E-Mail vpopov@fbras.ru, vpopov@inbi.ras.ru

University education and academic degrees:

1970-1975 Lomonosov Moscow State University, Department of Chemistry, Moscow, Russia, Diploma. Supervisor: Prof.A.Egorov
1978
Ph.D: Lomonosov Moscow State University, Department of Chemistry, 1978. Supervisor: Prof.A.Egorov
1988
Habilitation: A.N.Bach Institute of Biochemistry USSR Academy of Sciences
1997
Professor of Biochemistry A.N.Bach Institute of Biochemistry Russian Academy of Sciences
2011 Corresponding member of the Russian Academy of Sciences, Brunch of Nano- and Information Technologies

Academic Career:

2015-2019 Director of the Federal Research Centre of Biotechnology Russian Academy of Sciences, Moscow, Russia
2001-2015 Director of A.N.Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia
2009 – Present Supervisor of the Department “Protein Factory” of NBICS-Centre of the NRC “Kurchatov Institute”, Moscow, Russia
2008 – Present  Professor of the Moscow State University, Department of Biology, Chair of Bioengineering, Moscow, Russia
1991 – Present Head of the laboratory of Enzyme Engineering, A.N.Bach Institute of Biochemistry Russian Academy of Sciences, Moscow, Russia
1987-1991 Leading Research Scientist, Head of the Structure- Function of Macromolecules Research Group, A.N.Bach Institute of Biochemistry Russian Academy of Sciences, Moscow, Russia
1989 – 1990 Visiting Scientist, Institute of Microbiology and Plant Physiology, Free University of Berlin, FRG
1989 – 1989 Visiting Scientist, Institute of Catalysis, Madrid, Spain
1984 – 1985 Visiting Scientist, Department of Plant Sciences, King’s College, London, UK
1981 – 1987 Senior Research Scientist, A.N.Bach Institute of Biochemistry Russian Academy of Sciences, Moscow, Russia
1977 – 1981 Junior Research Scientist, Chemical Department Lomonosov Moscow State University, Division of Chemical Enzymology
1975 – 1977 Research Student, Chemical Department Lomonosov Moscow State University, Division of Chemical Enzymology

Honours and awards:

1997 State Prize of the Russian Government in the area of Science and Technology for “Development of technology for VOC abatement in industrial air emissions“
2010 State Prize of the Russian Government in the area of Science and Technology for “Development and commercialization of the biotechnological assays for solving socially important problems of screening of new-borns, control of drugs of abuse and food safety”

Membership in advisory boards (since):

1991 Scientific Council of A.N.Bach Institute of Biochemistry, Russian Acad.Sci., Head since 2002
1996 Scientific Council of the Russian Acad.Sci. on Biochemistry, Head since 2002
2001 Member of the Editorial Board of the journal Biochemistry (Russia)
2002 Editor-in-Chief of the journal Applied Biochemistry and Microbiology (Russia)
2003 FP6/7 National Contact Centre of Russia in the area of Biotechnology, Agriculture and Food, Head
2005 Representative of the Russian Federation in the OECD Working Party on Biotechnology
2011 Russian Technology Platform “Bioindustry and Bioresources, BioTech2030”, Coordinator
2012
  • Member of the Council awarding grants of the President of RF in the area of science and technology
  • Member of the Council awarding prizes of the Government of the Russian Federation in the area of science and technology
  • Member of the working group for the development of biotechnologies under the leadership of the Deputy Prime Minister of the Russian Federation
  • Member of the Scientific Council of NBICS-Centre of the NRC “Kurchatov Institute”
  • Interministerial committee on Technological development of the Presidium of the Presidential Council on Modernization of economy and innovative development of Russia, Member
  • Member of the Russian-German working group on biotechnology and the Bioeconomy
  • Deputy Editor-in-Chief of the journal “Achievements of Biological Chemistry”
  • Member of the editorial Board of the journal “Acta Naturae”
2015-2017 Member of the Expert Council of the Russian Scientific Fund


Main areas of research
:

Structural biology. Nanobiotechnologies. Enzymology, enzyme structure-function relationships and mechanisms. Protein and enzyme engineering, immobilised enzymes and cells. Biotechnology, biotransformations, and environment protection


Publications:

>300 peer-reviewed publications; Number of citations: 2235; h-index: 21 (http://expertcorps.ru/science/whoiswho/by_branch/bio-all 2017-12-31)

 

Selected publications:

  1. Popov V.O., Lamzin V.S. NAD+-dependent formate dehydrogenase. Biochem.J. (1994), v. 301, 625-643.
  2. Kutzenko A.S., Lamzin V.S., Popov V.O. Conserved supersecondary structural motif in NAD-dependent dehydrogenases. FEBS Letters (1998), v. 423, 105-109.
  3. Tishkov V.I., Popov V.O. Protein engineering of formate dehydrogenase. Biomolecular Engineering (2006), v. 23, 89–110. DOI: 10.1016/j.bioeng.2006.02.003
  4. Polyakov K.M., Boyko K.M., Tikhonova T.V., Slutsky A., Antipov A.N., Zvyagilskaya R.A., Popov A.N., Lamzin V.S. and Popov V.O. High-resolution structural analysis of novel octaheme cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thiolkalivibrio nitratireducens. J.Mol.Biol. (2009), v. 389, 846-862. DOI: 10.1016/j.jmb.2009.04.037
  5. Kravchenko I.V., Furalyov V.A., Lisitsina E.S., Popov V.O. Stimulation of mechano-growth factor expression by second messengers. Archives of Biochemistry and Biophysics (2011), v. 507, 323-331. DOI: 10.1016/j.abb.2010.12.028
  6. Bezsudnova E.Y., Boyko K.M., Polyakov K.M., Dorovatovskiy P.V., Stekhanova T.N., Gumerov V.M., Ravin N.V., Skryabin K.G., Kovalchuk M.V., Popov V.O. Structural insight into the molecular basis of polyextremophilicity of short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus. Biochemie (2012), v.94, N 12, 2628–2638. DOI: 10.1016/j.biochi.2012.07.024
  7. Trofimov A.A., Polyakov K.M., Lazarenko V.A., Popov A.N., Tikhonova T.V., Tikhonov А.V., Popov V.O. Structural study of the X-ray induced enzymatic reaction of octaheme cytochrome c nitrite reductase Acta Cryst. (2015) Sect.D, v.71, N5, 1087-94. DOI: 10.1107/S1399004715003053
  8. Irina V.Kravchenko, Vladimir A.Furalyov, Spyros Chatziefthimiou, Matthias Wilmanns, Vladimir O.Popov Induction of insulin-like growth factor 1 splice forms by subfragments of myofibrillar proteins Mol Cell Biochem. (2015) v.399, 69-77. DOI: 10.1016/j.mce.2014.08.010
  9. Ekaterina Yu. Bezsudnova, Tatiana E. Petrova, Anna V. Popinako, Mikhail Yu. Antonov, Tatiana N. Stekhanova and Vladimir O. Popov Intramolecular hydrogen bonding in the polyextremophilic short-chain dehydrogenase from the archaeon Thermococcus sibiricus and its close structural homologs Biochemie (2015) v.118, 82-89. DOI: 10.1016/j.biochi.2015.08.010
  10. Boyko, K; Rakitina, T; Korzhenevskiy,  D; Vlaskina, A; Agapova, Yu; Kamashev, D; Kleymenov, S; Popov V (2016) Structural basis of high thermal stability of histone-like HU protein from mollicute Spiroplasma melliferum KC3 Scientific Reports 6:36366. DOI: 10.1038/srep36366
  11. Ekaterina Yu. Bezsudnova, Tatiana N. Stekhanova, Alena Yu. Nikolaeva, Tatiana V. Rakitina, Anna V. Popinako, Konstantin M. Boyko and Vladimir O. Popov «Diaminopelargonic acid transaminase from Psychrobacter cryohalolentis is active towards (S)-(-)-1-phenylethylamine, aldehydes and α-diketones» Applied Microbiology and Biotechnology, 2018, doi:10.1007/s00253-018-9310-0. [Epub ahead of print]
  12. Konstantin M. Boyko, Timur N Baymukhametov, Yury M Chesnokov, Michael Hons, Sofya V Lushchekina, Petr V Konarev, Alexey V Lipkin, Alexandre L Vasiliev, Ph.D. Patrick Masson, Vladimir O Popov, Michail V Kovalchuk 3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MD. Biochimie. (2019), 156, 196-205. DOI: 10.1016/j.biochi.2018.10.017.

 

Публикации последних лет:

  1. E. Yu. Bezsudnova, K. M. Boyko, and V. O. Popov. Properties of Bacterial and Archaeal Branched-Chain Amino Acid Aminotransferases. Review. (2017) Biochemistry (Mosc), 82(13):1572-1591. doi: 10.1134/S0006297917130028.
  2. Tatiana N. Stekhanova, Andrey L. Rakitin, Andrey V. Mardanov, Ekaterina Yu. Bezsudnova, Vladimir O. Popov. A Novel highly thermostable branched-chain amino acid aminotransferase from the crenarchaeon Vulcanisaeta moutnovskia. Enz.Microb.Technol. (2017) v.96, 127-134, doi.org/10/1016/j.enzmictec.2016.10.002.
  3. Irina Kravchenko, Vladimir Furalyov, Vladimir Popov. Specific titin and myomesin domains stimulate myoblast proliferation. Biochemistry and Biophysics Reports (2017) v.9, 226–231.
  4. Popinako A., Antonov M., Tikhonov A., Tikhonova T., Popov V. Structural adaptations of octaheme nitrite reductase from haloalkaliphic Thioalkalivibrio bacteria to alkaline pH and high salinity. PLOS ONE (2017), v.12, N5, 1-17,
  5. Scheiblbrandner S, Breslmayr E, Csarman F, Paukner R, Führer J, Herzog PL, Shleev SV, Osipov EM, Tikhonova TV, Popov VO, Haltrich D, Ludwig R, Kittl R. Evolving stability and H-dependent activity of the high redox potential Botrytis aclada laccase for enzymatic fuel cells. Sci. Rep. (2017), 7(1):13688.
  6. Altukhov, DA; Talyzina, AA; Agapova, YK; Vlaskina, AV; Korzhenevskiy, DA; Bocharov, EV; Rakitina, TV; Timofeev, VI; Popov, VO. Enhanced conformational flexibility of the histone-like (HU) protein from Mycoplasma gallisepticum. Journal of biomolecular structure & dynamics (2018 ) v.36, N1, 45-53.
  7. Bezsudnova E.Yu., Dibrova D.V., Nikolaeva A.Yu., Rakitina T.V.. Popov V.O. Identification of branched-chain amino acid aminotransferases active forwards (R)-(+)-1-phenylethylamine among PLP fold IV transaminases. Journal of Biotechnology (2018), 271, 20-28.
  8. Bezsudnova E.Yu, Stekhanova T.N, Nikolaeva A.Yu., Rakitina T.V., Popinako A.V., Boyko K.M.and O. Popov V.O. Diaminopelargonic acid transaminase from Psychrobacter cryohalolentis is active towards (S)-(-)-1-phenylethylamine, aldehydes and α-diketones Applied Microbiology and Biotechnology. (2018), DOI: 10.1007/s00253-018-9310-0
  9. T. N. Baymukhametov, Y. M. Chesnokov, E. B. Pichkur, K. M. Boyko, T. V. Tikhonova, A. G. Myasnikov, A. L. Vasiliev, A. V. Lipkin, V. O. Popov, M. V. Kovalchuk. Three-dimensional structure оf cytochrome c nitrite reductase as determined by cryo-electron microscopy. Acta Naturae, 2018, V. 10, 3(38), 75-83.
  10. Nina N. Sykilinda, Alena Y. Nikolaeva, Mikhail M. Shneider, Dmitry V. Mishkin, Artem A. Patutin, Vladimir O. Popov, Konstantin M. Boyko, Natalia L. Klyachko, Konstantin A. Miroshnikov Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal Cell Wall Binding alpha-Helix. Viruses. (2018), 10(6), 309; https://doi.org/10.3390/v10060309
  11. Osipov E.M., Lilina A.V., Tsallagov S.I., Safonova T.N., Sorokin D.Y., Tikhonova T.V., Popov V.O Structure of the flavocytochrome c sulfide dehydrogenase associated with the copper-binding protein CopC from the haloalkaliphilic sulfur-oxidizing bacterium Thioalkalibrio paradoxus. Acta Cryst.D. (2018), D74 (Pt7), 632-642
  12. Petrova T.E., Boyko K.M., Nikolaeva A.Y., Stekhanova T.N., Gruzdev E.V., Mardanov A.V., Stroilov V.S., Littlechild J.A., Popov V.O., Bezsudnova E.Y. Structural characterization of geranylgeranyl pyrophosphate synthase GACE1337 from the hyperthermophilic archaeon Geoglobus acetivorans. Extremophiles. (2018), 2018, 22(6):877-888. DOI 10.1007/s00792-018-1044-5.
  13. Osipov EM, Lilina AV, Tsallagov SI, Safonova TN, Sorokin DY, Tikhonova TV, Popov VO. Structure of the flavocytochrome c sulfide dehydrogenase associated with the copper-binding protein CopC from the haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio paradoxusARh 1. Acta Crystallogr D Struct Biol. (2018) 74(Pt 7):632-642.
  14. Konstantin M. Boyko, Timur N Baymukhametov, Yury M Chesnokov, Michael Hons, Sofya V Lushchekina, Petr V Konarev, Alexey V Lipkin, Alexandre L Vasiliev, Ph.D. Patrick Masson, Vladimir O Popov, Michail V Kovalchuk 3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MD. Biochimie. (2019), 156, 196-205. DOI: 10.1016/j.biochi.2018.10.017.