Vladimir O. Popov

 

Vladimir O. Popov
Professor, Dr.Sci (Chemistry), Academician of the Russian Academy of Sciences
President 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
2019 Academician of the Russian Academy of Sciences, Brunch of Nano- and Information Technologies

Academic Career:

2020 – present President of the Research Centre of Biotechnology RAS
2019 – 2020
 Chief Scientific Adviser of the Directorate of the Federal Research Centre of Biotechnology Russian Academy of Sciences
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
1991 – 2001 Deputy Director of A.N.Bach Institute of Biochemistry, Russian Academy of Sciences, 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
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:

2022 Medal of the Order “For Merit to the Fatherland” II degree for contribution to the development of science and many years of diligent work
2018 Prize of the Russian Academy of Sciences named after E. S. Fedorov for the series of works “Structural biology of macromolecules important for biotechnology and medicine”
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”
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“

Membership in advisory boards (since):

  • Member of the Scientific and Technical Council of the Synchrotron and Neutron Research and Research Infrastructure Development Program for 2019-2027.
  • Member of the RAS Scientific Council on Global Environmental Problems
  • Member and Vice-Chairman of the RAS Council on Biotechnology
  • Member of the RAS Council on Life Sciences
  • Member of the RAS Council on Genetic Engineering
  • Member of the RAS Council on the priority of scientific and technological development “20G
  • Member of the Russian Biochemical Society Presidium
  • Member of Interdepartmental Commission on Technological Development under the Government Commission on Economic Modernization and Innovative Development of Russia
  • Co-head of the expert group of the Scientific Coordination Council of the Military Innovation Technopolis “ERA” of the Russian Ministry of Defence
  • Member of the Council for Grants of the President of the Russian Federation (RF Government)
  • Member of the Presidium of Council for the Awarding of Prizes of the Russian Government
  • Member of the Presidium Commission of the Higher Attestation Commission of the Ministry of Science and Higher Education of the Russian Federation
  • Coordinator of the Russian Technological Platform Biotech2030
  • Representative of the Russian Federation in the Organization for Economic Cooperation and Development (OECD) Working Group on Bio-, Nano-, and Convergent Technologies (BNCT)

Member of editorial boards of leading peer-reviewed scientific journals:

  • Editor-in-chief of the journal “Applied Biochemistry and Microbiology,” Deputy Editor-in-chief of the journal “Advances in Biological Chemistry”
  • Member of editorial board of the journal Biochemistry
  • Member of editorial board of the journal Acta Nature
  • Member of the editorial board of the journal “Russian Nanotechnologies


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:

>320 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. 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
  8. 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]
  9. 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.
  10. Tikhonova T.V., Sorokin D.Y., Hagen W.R., Khrenova M.G., Muyzer G., M., Rakitina T.V., Shabalin I.G., Trofimov A.A., Tsallagov S.I., Popov V.O. Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase. PNAS (2020), 117 (10) 5280-5290, DOI: 10.1073/pnas.1922133117
  11. Bonchuk A., Boyko K., Fedotova A., Nikolaeva A., Lushchekina S., Khrustaleva A., Popov V., Georgiev P. Structural basis of diversity and homodimerization specificity of zinc-finger-associated domains in Drosophila. Nucleic Acids Research (2021), v.49, N4, 2375-2389, DOI: 10.1093/nar/gkab061
  12. Tamara V. Tikhonova, Evgenii M. Osipov, Natalia I. Dergousova, Konstantin M. Boyko, Ivan M. Elizarov, Sergey N. Gavrilov, Maria G. Khrenova, Frank T. Robb, Anastasia Y. Solovieva, Elizaveta A. Bonch-Osmolovskaya, and Vladimir O. Popov Extracellular Fe (III) reductase structure reveals a modular organization enabling S-layer insertion and electron transfer to insoluble substrates. Structure (2023), V.31, N2, 174-184, DOI: 10.1016/j.str.2022.12.010