Yuri A. Ovchinnikov


PeriodCountry, cityEducation institutionAdditional info
1952–1957 Russia, Moscow M.V. Lomonosov M.V. Lomonosov Moscow State University (chemical faculty) MS in Chemistry
1957–1961 Russia, Moscow M.V. Lomonosov Moscow State University (chemical faculty) PhD in Chemistry
1964 Switzerland, Zurich Zurich High Technical School, Laboratory of Nobel prize winner Prof. V. Prelog Visitor researcher
1966 Russia, Moscow D.Sc. in Chemistry
Russia, Moscow Awarded professor degree in chemistry

Selected publications

  1. Ovchinnikov Yu.A., Abdulaev N.G., Zolotarev A.S., Artamonov I.D., Bespalov I.A., Dergachev A.E., Tsuda M. (1988). Octopus rhodopsin. Amino acid sequence deduced from cDNA. FEBS Lett. 232 (1), 69–72 [+]

    The primary structure of rhodopsin from the octopus Paroctopus defleini has been determined by parallel analysis of the protein and corresponding cDNA. The amino acid sequence is most similar to the recently cloned Drosophila opsins. Similarities to bovine and human opsins are also evident. The transmembrane topology of octopus rhodopsin is discussed.

  2. Arseniev A.S., Bystrov V.F., Lomize A.L., Ovchinnikov Yu.A. (1985). 1H-NMR study of gramicidin A transmembrane ion channel. Head-to-head right-handed, single-stranded helices. FEBS Lett. 186 (2), 168–174 [+]

    The structure of [Val1] gramicidin A incorporated into sodium dodecyl-d25 sulphate micelles has been studied by two-dimensional proton NMR spectroscopy. Analysis of nuclear Overhauser effects, spin-spin couplings and solvent accessibility of NH groups show that the conformation of the Na+ complex of gramicidin A in detergent micelles, which in many ways mimic the phospholipid bilayer of biomembranes, is an N-terminal to N-terminal (head-to-head) dimer Image formed by two right-handed, single-stranded β6.3 helices with 6.3 residues per turn, differing from Urry's structure by handedness of the helices.

  3. Ovchinnikov Yu.A., Lipkin V.M., Shuvaeva T.M., Bogachuk A.P., Shemyakin V.V. (1985). Complete amino acid sequence of gamma-subunit of the GTP-binding protein from cattle retina. FEBS Lett. 179 (1), 107–10 [+]

    The complete amino acid sequence of the gamma-subunit of the GTP-binding protein from cattle retina has been established. The polypeptide chain of the gamma-subunit consists of 69 amino acid residues and contains the unusual sequence Cys35-Cys36. The Mr of the gamma-subunit is 8008.7.

  4. Ovchinnikov Yu.A., Bystrov V.F., Ivanov V.T. (1984). NMR solution conformation of gramicidin A double helix. FEBS Lett. 165 (1), 51–56 [+]

    The conformation of species 3 of Val-gramicidin A in dioxane has been determined by two-dimensional NMR spectroscopy. It is presented by the left handed up arrow, down arrowππ5.6LD double helix, a suitable model of an ion permeable pore across the membrane matrix.

  5. Овчинников Ю.А., Ефимов В.А., Чахмачёва О.В., Зайцева Е.М., Арсенян С.Г., Новохатский А.С., Аспетов Р.Д., Кузнецов В.П. (1983). Химико-ферментативный синтез и клонирование гена проинсулина человека. Докл. АН СССР. 18 (1), 48–49 ID:148
  6. Ovchinnikov Yu.A., Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Salomatina I.S., Shuvaeva T.M., Lipkin V.M., Sverdlov E.D. (1982). The primary structure of E. coli RNA polymerase, Nucleotide sequence of the rpoC gene and amino acid sequence of the beta'-subunit. Nucleic Acids Res. 10 (13), 4035–44 [+]

    The primary structure of the E. coli rpoC gene (5321 base pairs) coding the beta'-subunit of RNA polymerase as well as its adjacent segment have been determined. The structure analysis of the peptides obtained by cleavage of the protein with cyanogen bromide and trypsin has confirmed the amino acid sequence of the beta'-subunit deduced from the nucleotide sequence analysis. The beta'-subunit of E. coli RNA polymerase contains 1407 amino acid residues. Its translation is initiated by codon GUG and terminated by codon TAA. It has been detected that the sequence following the terminating codon is strikingly homologous to known sequences of rho-independent terminators.

  7. Ovchinnikov Yu.A., Abdulaev N.G., Feigina M.Y.u., Kiselev A.V., Lobanov N.A. (1979). The structural basis of the functioning of bacteriorhodopsin: an overview. FEBS Lett. 100 (2), 219–224 [+]

    The present paper is a summing up of our studies, begun in 1976, that have resulted in the complete structural elucidation of bacteriorhodopsin, the first of the true membrane proteins for which this has been successfully accomplished. The results have opened wide perspectives for further work on the mode of action of this membrane-located proton pump and the approach can be of help in the studies of other membrane proteins.

  8. Bystrov V.F., Gavrilov Yu.D., Ivanov V.T., Ovchinnikov Yu.A. (1977). Refinement of the solution conformation of valinomycin with the aid of coupling constants from thr 13C-nuclear-magnetic-resonance spectra. Eur. J. Biochem. 78 (1), 63–82 [+]

    he C'= O and Cα signals in the 13C nuclear magnetic resonance (NMR) spectra of valinomycin have been assigned and the vicinal 1H…13C coupling constants have been determined by double and triple heteronuclear resonance. In conjunction with the vicinal H-NCα-H and H-CαCβ-H proton-proton constants, the results led to unequivocal determination of the torsion angles φ and of the population distribution of the Cα-Cβ rotational states. The Φ torsion angles for the hydroxy acid residues were estimated from the vicinal 1H-CαC'-15N constants. The combined data permitted refinement of the conformational states of valinomycin in different solvents. For the KS+ complex of valinomycin the observed couplings are in complete accord with the conformations we had earlier proposed for solutions and that had also been established by X-ray analysis. In the 13C spectra of the valinomycin-Tl+ complex 13C…203,205Tl+ spin-spin couplings were observed for the l and d-valine carbonyls, unequivocal proof of the donor-acceptor interaction with the cation. In media of weak polarity (cyclohexane, chloroform) the conformation of the valinomycin molecule is similar to that of the K+ complex. In such a 'bracelet' structure formed by six fused β-turns of type II and II', the amino acid carbonyls are axial with certain inclination towards the symmetry axis. On formation of a 1:1 complex with a cation the carbonyl orientation changes, now bending towards the center of the molecular cavity. In the 'propeller' conformation, predominant in solvents of medium polarity (for instance CCl4/(C2H3)2SO, 3/1) the three β-turns are of type II. The 1H and 13C chemical shifts are interpreted in terms of conformational changes in the valinomycin molecule, intermolecular and intramolecular hydrogen bonds and interaction with the metal cation.

  9. Овчинников Ю.А., Липкин В.М., Модянов Н.Н., Чертов О.Ю., Смирнов Ю.В., Хохряков В.С., Шуваева Т.М. (1977). ДНК-зависимая РНК-полимераза E.coli. Полная аминокислотная последовательность альфа-субъединицы. Биоорг. хим. 3 (1), 283–286 ID:147
  10. Ovchinnikov Yu.A., Lipkin V.M., Modyanov N.N., Chertov O.Y., Smirnov Y.V. (1977). Primary structure of alpha-subunit of DNA-dependent RNA polymerase from Escherichia coli. FEBS Lett. 76 (1), 108–11 [+]

    Transcription of genetic information in bacterial cells is mediated by DNA-dependent RNA polymerase (ribonucleoside-triphosphate:RNA nucleotidyltransferase, EC [ 11. The enzyme from E. coli
    (mol. wt 500 000) has been shown to possess a complex structure [2] consisting of two large subunits, /?
    and 0’ (mol. wt 155 000 and 16.5 000, respectively), two a-subunits (mol. wt 40 000) and initiation factor,
    u (mol. wt 90 000). Its structural complexity is paralleled by the multistep nature of the transcription
    process. Only limited information on the role of the individual subunits in the functioning of RNA polymerase
    is available, owing in part to our lack of knowledge of its primary and spatial structure. We have, therefore,
    undertaken an investigation into the primary structure of DNA-dependent RNA polymerase from
    E. coli B. In the study reported here we have determined the complete amino acid sequence of the RNA poly
    merase a-subunit (see [3] ) using a variety of degradation methods and i4C-enriched amino acid residues
    for facilitating detection and isolation of the fragments. The polypeptide chain of the o-subunit has mol. w
    36 512 and consists of 329 amino acid residues. In a comparative study of the peptide compositions of
    various bacterial polymerase a-subunits it has been shown by peptide mapping that they are evolutionarily
    conservative proteins [4].

  11. Ovchinnikov Y.A., Ivanov V.T., Evstratov A.V., Sumskaya L.V., Melnik E.I., Chumburidze T.S., Portnova S.L., Balashova T.A. (1973). Sandwich complexes as a functional form of the enniatin ionophores. FEBS Lett. 36 (1), 65–71 [+]

    The ability of the enniatin cyclodepsipeptides (CDP) (fig. 1) to form complexes with alkali metal ions (M+) and induce ionic permeability in artificial and biological membranes has been described in a number of papers [ 1,2]. The complexes were found to be equimolar in both solutions and in the crystalline state; by analogy with valinomycin and the nactins the role of the M+ carriers across the membrane was ascribed to them [3,49. In the present paper evidence is produced showing that an important part in the functioning of this group of ionophores is played by complexes with 2: 1 and 3:2 macrocycle:cation ratios.

  12. Ovchinnikov Yu.A., Egorov C.A., Aldanova N.A., Feigina M.Y., Lipkin V.M., Abdulaev N.G., Grishin E.V., Kiselev A.P., Modyanov N.N., Braunstein A.E., Polyanovsky O.L., Nosikov V.V. (1973). The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heart. FEBS Lett. 29 (1), 31–34 [+]

    Aspartate aminotransferase (L-aspartate: 2-oxo-glutarate aminotransferase, EC is one of the principal pyridoxal-P-containing enzymes that catalyse the transamination reactions [3] representing key steps
    at the intersection between the metabolic pathways of amino acids and dicarboxylic acids.
    Although the catalytic mechanism of aspartate aminotransferase has been investigated at the level of substrate-coenzyme models [4], its elucidation in detail requires knowledge of the enzyme’s structure, considering, in particular, that the very high rates of the enzymic process are determined by the structural peculiarities of the specific protein(apoenzyme) of the aspartate aminotransferase. Accordingly, we embarked
    on the task of elucidating the amino acid sequence of this enzyme. In the present paper the concluding stage
    of the work is reported*. The object chosen for study was the aspartate aminotransferase
    of the cytosol of pig heart; the enzyme, which is different from the mitochondrial isozyme
    [5,6] was prepared by a previously reported procedure [7]. The enzyme is a complex dimeric protein of
    high molecular weight; each of the associated subunits consists of a single polypeptide chain and has no disulfide bridges. Indirect evidence (amino acid composition, analysis of N-terminal residues, and peptide maps) testified to the identity of the two subunits [8].

  13. Bystrov V.F., Ivanov V.T., Portnova S.L., Balashova T.A., Ovchinnikov Yu.A. (1973). Refinement of the angular dependence of the peptide vicinal NH-CaH coupling constant. Tetrahedron 29 (6), 873–877 [+]

    The refined dependence of the peptide NHCαH vicinal coupling constant on the dihedral angle θ have been derived on the basis of the accumulated experimental data. The mean permissible values (in Hz) are approximated by 3JNHCH = 9·4 cos2 θ - 1·1 cos θ + 0·4 An analogous relationship for the sum of two vicinal NH-CαH2 coupling constants in the glycyl residue have been calculated from the above dependence. Measurements on N-methylacetamide in various solvents and in the presence of an alkali salt showed the vicinal constant NH-CH to vary by not more than ± 3%. Some of the other proposed 3JNHCH(θ) dependencies give too low values for the cis-oriented NH and CαH bonds. This may be due to the fact that in these correlations the data for compounds with cis-amide bonds have been used for 0° - θ - 90° region of the dependence.

  14. Ivanov V.T., Shemyakin M.M., Ovchinnikov Yu.A. (1969). Topochemische Untersuchungen an Peptidsystemen. Angew. Chemie 14, 523–529 ID:168
  15. Ovchinnikov Yu.A., Shemyakin M.M., Ivanov V.T., Antonov V.K., Vinogradova E.I., Shkrob A.M., Malenkov G.G., Evstratov A.V., Laine I.A., Melnik E.I., Ryabova I.D. (1969). Cyclodepsipeptides as chemical tool for studying ionic transport through membranes. J. Membr. Biol. 1, 402–403 [+]

    This paper reports a study of the chemistry of valinomycin, enniatins and related membrane-active depsipeptides that increase alkali metal ion permeability of model and biological membranes. The antimicrobial activity of these compounds and thir effect on membranes has been correlated with their cation-complexing ability. the complexing reaction has been studied by spectropolarimetric studies have revealed coexistence of conformers of the cyclopeptides and conductometric methods.  Nuclear magnetic resonance, optical rotatory dispersion, and infrared spectrophotometric studies have revealed the coexistence ofconformers of the cyclodepsipeptides in solution and have led to elucidation of the spatial structure of valinomycin, enniatin B and their K+ complexes. The effect of the conformational properties of the cyclodepsipeptides on their complexation efficiency and selectivity, surface-active properties and behavior towards phospholipid monolayers, bimolecular phospholipid membranes and a number of biological membrane systems has been ascertained. The studies have clearly shown the feasibility of using cyclodepsipeptides with predetermined structural and conformational parameters as chemical tools for membrane studies. It is suggested that the principle of conformation-dependent cation binding through ion-dipole interactions may possibly lie at the basis of the mode of action of systems governing the natural ion permeability in biological membranes.

  16. Овчинников Ю.А. (1968). Связь между структурой и биологической функцией в пептидных системах (новый подход к изучении проблемы). Вестн. АН СССР 7, 43–50 ID:140
  17. Shemyakin M.M., Ovchinnikov Yu.A., Kiryushkin A.A., Vinogradova E.I., Miroshnikov A.I., Alakhov Yu.B., Lipkin V.M., Shvetsov Yu.B., Wulfson N.S., Rosinov B.V., Bochkarev V.N., Burikov V.M. (1966). Mass spectrometric determination of the amino-acid sequence of peptides. Nature 211 (5047), 361–6 [+]

    New method of determination polypeptide amino acids sequenses with mass-spectoscopy of acyl ethers. This method base on peptide fragmentation with localizing positive charge on N-acyl fragments.

  18. Ovchinnikov Yu.A., Shemyakin M.M., Kiryushkin A.A., Kozhevnikova I.V. (1965). Synthesis of peptides in solution on polymeric support: 1. Synthesis of glycylglycyl-L-leucylglycine. Tetrahedron Lett. 27, 2323–2327 ID:138
  19. Ovchinnikov Yu.A., Gerlach H., Prelog V. (1964). Cycloenantiomerie und Cyclodiastereomeria: 2. Über cycloenantiomere cyclo-Hexaalanyle und ein cycloenantiomeres cyclo-Diglycyl-tetraalanyl. Helv. chim. Acta. 47 (8), 2294–2302 ID:137
  20. Овчинников Ю.А., Арбузов Ю.А., Берлин Ю.А., Волков Ю.П., Колосов М.Н., Се Ю., Тао Ч., Шемякин М.М. (1961). Исследование путей синтеза тетрациклинов. Антибиотики 7, 585–594 ID:136