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Your search keyword '"Klyachko, N."' showing total 333 results
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333 results on '"Klyachko, N."'

78. INCREASING PERMEABILITY OF OUTER MEMBRANE OF E.COLI UNDER ULTRA-LOW FREQUENCY ALTERNATING MAGNETIC FIELD IN THE PRESENCE OF MAGNETIC NANOPARTICLES

Author

Nikitin, A., additional, Dagaev, N., additional, Gribanovsky, S., additional, Ghigachev, A., additional, Golovin, D., additional, Legotsky, S., additional, Veselov, M., additional, Vlasova, K., additional, Lapankova, A., additional, Miroshnikov, K., additional, Belogurova, N., additional, Zaitseva, E., additional, Kabanov, A., additional, Majouga, A., additional, Golovin, Yu., additional, and Klyachko, N., additional

Published
2020
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92. Electrochemistry of chemically trapped dimeric and monomeric recombinant horseradish peroxidase

Author

Ignatenko, O. V., Sjölander, A., Hushpulian, D. M., Kazakov, S. V., Ouporov, I. V., Chubar, T. A., Poloznikov, A. A., Ruzgas, Tautgirdas, Tishkov, V. I., Gorton, L., Klyachko, N. L., Gazaryan, I. G., Ignatenko, O. V., Sjölander, A., Hushpulian, D. M., Kazakov, S. V., Ouporov, I. V., Chubar, T. A., Poloznikov, A. A., Ruzgas, Tautgirdas, Tishkov, V. I., Gorton, L., Klyachko, N. L., and Gazaryan, I. G.

Abstract

Native horseradish peroxidase (nHRP) exists in the aggregated form in concentrated water solutions as shown by dynamic light scattering (DLS). This is in contrast to recombinant horseradish peroxidase (recHRP) which mainly exists as a dimer. The native enzyme aggregates could be broken into the particles of nm-size only under the conditions of high ionic strength (0.5-1 M NaCl). Chemical cross-linking of recHRP with glutaraldehyde in water solutions yields 40% of the dimer. The chemically trapped dimeric and monomeric forms of recHRP were separated by gel-filtration, their substrate specificity towards a number of organic substrates compared. Parameters of direct and mediated electron transfer on graphite electrodes catalyzed by both preparations were analyzed. The difference in behavior of the monomeric and dimeric enzyme forms observed in electrochemical experiments was interpreted as a result of a “double” coverage of the electrode surface with the molecules of cross-linked dimeric enzyme, in contrast to both modified monomeric and original, unmodified recHRP providing “monolayer” coverage. In addition to the stabilization effects achieved due to enzyme surface modification with glutaraldehyde, the “double” coverage doubles the enzyme activity per surface unit.

Published
2013

96. Use of a Reverse Micelle System for Study of Oligomeric Structure of NAD+-Reducing Hydrogenase from Ralstonia eutropha H16.

Author

Tikhonova, T. V., Kurkin, S. A., Klyachko, N. L., and Popov, V. O.

Subjects
REVERSED micelles, OLIGOMERS, POLYMERS, HYDROGENASE, OXIDOREDUCTASES, RALSTONIA
Abstract

Inclusion of an oligomeric enzyme, NAD+-dependent hydrogenase from the hydrogen-oxidizing bacterium Ralstonia eutropha, into a system of reverse micelles of different sizes resulted in its dissociation into catalytically active heterodimers and subunits, which were characterized in reactions with various substrates. It was found that: 1) the native tetrameric form of this enzyme catalyzes all types of studied reactions; 2) hydrogenase dimer, HoxHY, is a minimal structural unit catalyzing hydrogenase reaction with an artificial electron donor, reduced methyl viologen; 3) all structural fragments containing FMN and NAD+/NADH-binding sites exhibit catalytic activity in diaphorase reactions with one- and two-electron acceptors; 4) small subunits, HoxY and HoxU also exhibit activity in diaphorase reactions with artificial acceptors. These results can be considered as indirect evidence that the second FMN molecule may be associated with one of the small subunits (HoxY or HoxU) of the hydrogenase from R. eutropha. [ABSTRACT FROM AUTHOR]

Published
2005
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