Научные интересы

Структурная биология. Нанобиотехнологии. Энзимология, механизм действия, структура и функция ферментов. Белковая инженерия. Инженерная энзимология. Биотрансформации. Биотехнология и охрана окружающей среды.

Научные публикации

•‎ 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) v.102, 9621-9633, DOI: 10.1007/s00253-018-9310-0 https://pubmed.ncbi.nlm.nih.gov/30178202/ IF 5.56
•‎ 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), 632-64.DOI: 10.1107/S2059798318005648 https://pubmed.ncbi.nlm.nih.gov/29968673/ IF 5.699
•‎ Bezsudnova E.Y., Boyko K.M., Nikolaeva A.Y., Zeifman Y.S., Rakitina T.V., Suplatov D.A., Popov V.O. Biochemical and structural insights into PLP fold IV transaminase from Thermobaculum terrenum. Biochimie. (2019) v.158, 130-138, DOI: 10.1016/j.biochi.2018.12.017, https://pubmed.ncbi.nlm.nih.gov/30599183/ IF 4.372
•‎ Isupov M.N., Boyko K.M., Sutter J.-M., James P., Sayer C., Schmidt M., Schoenheit P., Nikolaeva A.Y., Stekhanova T.N., Mardanov A.V., Ravin N.V., Bezsudnova E.Y., Popov V.O., Littlechild J. Thermostable branched-chain amino acid transaminases from the Archaea Geoglobus acetivorans and Archaeoglobus fulgidus: biochemical and structural characterization. Front.Bioeng.Biotechnol. (2019) v.7, article 7, DOI: 10.3389/fbioe.2019.00007 https://pubmed.ncbi.nlm.nih.gov/30733943/ IF 6.064
•‎ Boyko K.M., Baymukhametov T.N., Chesnokov Yu.M., Hons M., Lushchekina S.V., Konarev P.V., Lipokin A.V., Vasiliev A.L., Masson P., Popov V.O., Kovalchuk M.V. 3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MD. Biochimie (2019) v.156, 196-205.DOI: 10.1016/j.biochi.2018.10.017, https://pubmed.ncbi.nlm.nih.gov/30385318/ IF 4.372
•‎ Tsallagov S.I., Sorokin D.Y., Tikhonova T.V., Popov V.O., Muyzer G. Comparative genomics of Thiohalobacter thiocyanaticus HRh1T and Guyparkeria sp. SCN-R1, halophilic chemolithoautotrophic sulfur-oxidizing gammaproteobacteria capable of using thiocyanate as energy source. Fronters in Microbiology (2019) v.10, article 898, DOI:10.3389/fmicb.2019.00898, https://pubmed.ncbi.nlm.nih.gov/31118923/ IF 6.064
•‎ Boyko K., Kryukova M., Petrovskaya L.,Nikolaeva A., Korzhenevsky D., Novototskaya-Vlasova K., Rivkina E., Dolgikh D., Kirpichnikov M., Popov V. Crystal structure of PMGL2 esterase from the hormonesensitive lipase family with GCSAG motif around the catalytic serine. PLOS One (2020) v.15, N1:e0226838, DOI: 10.1371/journal.pone.0226838 https://pubmed.ncbi.nlm.nih.gov/31990908/ IF 3.752
•‎ 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, https://pubmed.ncbi.nlm.nih.gov/32094184/ IF 12.77
•‎ Artem Bonchuk, Sofia Kamalyan, Sofia Mariasina, Konstantin Boyko, Vladimir Popov, Oksana Maksimenko, Pavel Georgiev. N-terminal domain of the architectural protein CTCF has similar structural organization and ability to self-association in bilaterian organisms". Scientific Reports (2020) N10: 2677, DOI: 10.1038/s41598-020-59459-5, https://pubmed.ncbi.nlm.nih.gov/32060375/ IF 4.996
•‎ 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, https://pubmed.ncbi.nlm.nih.gov/33638995/ IF 19.16
•‎ Gavrilov S.N., Zavarzina D.G., Elizarov I.M., Tikhonova T.V., Dergousova N.I., Popov V.O., Lloyd J.R., Knight D., EL-Naggar M.Y., Pirbadian S., Leung K.M., Robb F.T., Zakhartsev M.V., Bretschger O., Bonch-Osmolovskaya E.A. Novel extracellular election transfer channels in a gram-positive thermophilic bacterium. Front Microbiol. (2021), v.11, 597818, DOI: 10.3389/fmicb.2020.597818, https://pubmed.ncbi.nlm.nih.gov/33505370/ IF 6.064
•‎ Bezsudnova E.Yu., Nikolaeva A.Yu., Bakunova A.K., Rakitina T.V., Suplatov D.A., Popov V.O., Boyko K.M. Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum. PLoS ONE (2021), v.16, N7, e0255098, DOI: 10.1371/journal.pone.0255098, https://pubmed.ncbi.nlm.nih.gov/34324538/ IF 3.752
•‎ Bakunova A.K., Nikolaeva A.Yu., Rakitina T.V., Isaikina T.Y., Khrenova M.G., Boyko K.M., Popov V.O., Bezsudnova E.Yu. The uncommon active site of D-amino acid transaminase from Haliscomenobacter hydrossis: biochemical and structural insights into the new enzyme. Molecules (2021), 26(16), 5053, DOI: 10.3390/molecules26165053, https://pubmed.ncbi.nlm.nih.gov/34443642/ IF 4.927
•‎ Sabirov M., Popovich A., Boyko K., Nikolaeva A., Kyrchanova O., Maksimenko O., Popov V., Georgiev P., Bonchuk A. Mechanisms of CP190 interaction with architectural proteins in Drosophila melanogaster. International Journal of Molecular Sciences. (2021), v.22, N 23, 12400, DOI:10.3390/ijms222212400, https://pubmed.ncbi.nlm.nih.gov/34830280/ IF 6.208
•‎ Bonchuk A.N., Boyko K.M., Nikolaeva A.Y., Burtseva A.D., Popov V.O., Georgiev P.G. Structural insights into highly similar spatial organization of zinc-finger associated domains (ZAD) with a very low sequence similarity. Structure (2022) v.30, 1-12, DOI: 10.1016/j.str.2022.04.009, https://pubmed.ncbi.nlm.nih.gov/35580610/ IF 5.006

Премии и награды

•‎ Премия правительства России за достижения в области науки и техники “Создание технологии биологической очистки воздуха от техногенных выбросов летучих органических соединений”, 1997 г.
•‎ Премия правительства России за достижения в области науки и техники «Создание и внедрение в отечественную практику биотехнологических методов анализа для решения социально значимых задач неонатального скрининга, контроля наркопотребления и безопасности продуктов питания», 2010 г.
•‎ Премия имени Е. С. Федорова (премия РАН) за цикл работ «Структурная биология макромолекул, значимых для биотехнологии и медицины», 2018 г.

Персональные профили исследователя

•‎ Web of Science: F-8810-2014.
•‎ Scopus: 7404534215.
•‎ РИНЦ: 80944.
•‎ ORCID: 0000-0002-0133-7962.