Search Results - "Tikhonova, Tamara V"

Trichlorobacter ammonificans, a dedicated acetate-dependent ammonifier with a novel module for dissimilatory nitrate reduction to ammonia by Sorokin, Dimitry Y., Tikhonova, Tamara V., Koch, Hanna, van den Berg, Eveline M., Hinderks, Renske S., Pabst, Martin, Dergousova, Natalia I., Soloveva, Anastasia Y., Kuenen, Gijs J., Popov, Vladimir O., van Loosdrecht, Mark C. M., Lücker, Sebastian

“…Dissimilatory nitrate reduction to ammonia (DNRA) is a common biochemical process in the nitrogen cycle in natural and man-made habitats, but its significance…”
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Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase by Tikhonova, Tamara V., Sorokin, Dimitry Y., Hagen, Wilfred R., Khrenova, Maria G., Muyzer, Gerard, Rakitina, Tatiana V., Shabalin, Ivan G., Trofimov, Anton A., Tsallagov, Stanislav I., Popov, Vladimir O.

“…Biocatalytic copper centers are generally involved in the activation and reduction of dioxygen, with only few exceptions known. Here we report the discovery…”
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Unusual Cytochrome c552 from Thioalkalivibrio paradoxus: Solution NMR Structure and Interaction with Thiocyanate Dehydrogenase by Britikov, Vladimir V., Bocharov, Eduard V., Britikova, Elena V., Dergousova, Natalia I., Kulikova, Olga G., Solovieva, Anastasia Y., Shipkov, Nikolai S., Varfolomeeva, Larisa A., Tikhonova, Tamara V., Timofeev, Vladimir I., Shtykova, Eleonora V., Altukhov, Dmitry A., Usanov, Sergey A., Arseniev, Alexander S., Rakitina, Tatiana V., Popov, Vladimir O.

“…The search of a putative physiological electron acceptor for thiocyanate dehydrogenase (TcDH) newly discovered in the thiocyanate-oxidizing bacteria…”
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Novel Extracellular Electron Transfer Channels in a Gram-Positive Thermophilic Bacterium by Gavrilov, Sergey N, Zavarzina, Daria G, Elizarov, Ivan M, Tikhonova, Tamara V, Dergousova, Natalia I, Popov, Vladimir O, Lloyd, Jonathan R, Knight, David, El-Naggar, Mohamed Y, Pirbadian, Sahand, Leung, Kar Man, Robb, Frank T, Zakhartsev, Maksim V, Bretschger, Orianna, Bonch-Osmolovskaya, Elizaveta A

“…Biogenic transformation of Fe minerals, associated with extracellular electron transfer (EET), allows microorganisms to exploit high-potential refractory…”
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Probing the Role of a Conserved Phenylalanine in the Active Site of Thiocyanate Dehydrogenase by Varfolomeeva, Larisa A, Solovieva, Anastasia Yu, Shipkov, Nikolai S, Kulikova, Olga G, Dergousova, Natalia I, Rakitina, Tatiana V, Boyko, Konstantin M, Tikhonova, Tamara V, Popov, Vladimir O

“…Copper-containing enzymes catalyze a broad spectrum of redox reactions. Thiocyanate dehydrogenase (TcDH) from Thioalkalivibrio paradoxus Arh1 enables the…”
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Comparative Genomics of Thiohalobacter thiocyanaticus HRh1T and Guyparkeria sp. SCN-R1, Halophilic Chemolithoautotrophic Sulfur-Oxidizing Gammaproteobacteria Capable of Using Thiocyanate as Energy Source by Tsallagov, Stanislav I., Sorokin, Dimitry Y., Tikhonova, Tamara V., Popov, Vladimir O., Muyzer, Gerard

“…The genomes of Thiohalobacter thiocyanaticus and Guyparkeria (formerly known as Halothiobacillus ) sp. SCN-R1, two gammaproteobacterial halophilic…”
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High-Resolution Structural Analysis of a Novel Octaheme Cytochrome c Nitrite Reductase from the Haloalkaliphilic Bacterium Thioalkalivibrio nitratireducens by Polyakov, Konstantin M., Boyko, Konstantin M., Tikhonova, Tamara V., Slutsky, Alvira, Antipov, Alexey N., Zvyagilskaya, Renata A., Popov, Alexandre N., Bourenkov, Gleb P., Lamzin, Victor S., Popov, Vladimir O.

“…Bacterial pentaheme cytochrome c nitrite reductases (NrfAs) are key enzymes involved in the terminal step of dissimilatory nitrite reduction of the nitrogen…”
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Thiocyanate hydrolase, the primary enzyme initiating thiocyanate degradation in the novel obligately chemolithoautotrophic halophilic sulfur-oxidizing bacterium Thiohalophilus thiocyanoxidans by Bezsudnova, Ekaterina Yu, Sorokin, Dimitry Yu, Tikhonova, Tamara V., Popov, Vladimir O.

“…Thiohalophilus thiocyanoxidans is a first halophilic sulfur-oxidizing chemolithoautotrophic bacterium capable of growth with thiocyanate as an electron donor…”
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Molecular mechanism of thiocyanate dehydrogenase at atomic resolution by Varfolomeeva, Larisa A., Shipkov, Nikolai S., Dergousova, Natalia I., Boyko, Konstantin M., Khrenova, Maria G., Tikhonova, Tamara V., Popov, Vladimir O.

“…Some sulfur-oxidizing bacteria playing an important role in global geochemical cycles utilize thiocyanate as the sole source of energy and nitrogen. In these…”
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Extracellular Fe(III) reductase structure reveals a modular organization enabling S-layer insertion and electron transfer to insoluble substrates by Tikhonova, Tamara V., Osipov, Evgenii M., Dergousova, Natalia I., Boyko, Konstantin M., Elizarov, Ivan M., Gavrilov, Sergey N., Khrenova, Maria G., Robb, Frank T., Solovieva, Anastasia Y., Bonch-Osmolovskaya, Elizaveta A., Popov, Vladimir O.

“…The thermophilic anaerobic Gram-positive bacterium Carboxydothermus ferrireducens utilizes insoluble Fe(III) oxides as electron acceptors in respiratory…”
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Evolving stability and pH-dependent activity of the high redox potential Botrytis aclada laccase for enzymatic fuel cells by Scheiblbrandner, Stefan, Breslmayr, Erik, Csarman, Florian, Paukner, Regina, Führer, Johannes, Herzog, Peter L., Shleev, Sergey V., Osipov, Evgeny M., Tikhonova, Tamara V., Popov, Vladimir O., Haltrich, Dietmar, Ludwig, Roland, Kittl, Roman

“…Fungal high redox potential laccases are proposed as cathodic biocatalysts in implantable enzymatic fuel cells to generate high cell voltages. Their…”
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Catalytic Properties of Flavocytochrome c Sulfide Dehydrogenase from Haloalkaliphilic Bacterium Thioalkalivibrio paradoxus by Tikhonova, Tamara V., Lilina, Anastasiya V., Osipov, Evgenii M., Shipkov, Nikolay S., Dergousova, Nataliya I., Kulikova, Olga G., Popov, Vladimir O.

“…Flavocytochrome c sulfide dehydrogenase (FCC) is one of the central enzymes of the respiratory chain in sulfur-oxidizing bacteria. FCC catalyzes oxidation of…”
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Structure of the flavocytochrome c sulfide dehydrogenase associated with the copper‐binding protein CopC from the haloalkaliphilic sulfur‐oxidizing bacterium Thioalkalivibrio paradoxusARh 1 by Osipov, Eugeny M., Lilina, Anastasia V., Tsallagov, Stanislav I., Safonova, Tatyana N., Sorokin, Dimitry Y., Tikhonova, Tamara V., Popov, Vladimir O.

“…Flavocytochrome c sulfide dehydrogenase from Thioalkalivibrio paradoxus (TpFCC) is a heterodimeric protein consisting of flavin‐ and monohaem c‐binding…”
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Contrasting catalytic profiles of multiheme nitrite reductases containing CxxCK heme-binding motifs by Doyle, Rose-Marie A. S., Marritt, Sophie J., Gwyer, James D., Lowe, Thomas G., Tikhonova, Tamara V., Popov, Vladimir O., Cheesman, Myles R., Butt, Julea N.

“…The multiheme cytochromes from Thioalkalivibrio nitratireducens (TvNiR) and Escherichia coli (EcNrfA) reduce nitrite to ammonium. Both enzymes contain…”
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Molecular and catalytic properties of a novel cytochrome c nitrite reductase from nitrate-reducing haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio nitratireducens by Tikhonova, Tamara V., Slutsky, Alvira, Antipov, Alexey N., Boyko, Konstantin M., Polyakov, Konstantin M., Sorokin, Dimitry Y., Zvyagilskaya, Renata A., Popov, Vladimir O.

“…A highly active cytochrome c nitrite reductase from the haloalkaliphilic sulfur-oxidizing non-ammonifying bacterium Tv. nitratireducens strain ALEN 2 (TvNiR)…”
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Structures of complexes of octahaem cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens with sulfite and cyanide by Trofimov, Anton A., Polyakov, Konstantin M., Boyko, Konstantin M., Tikhonova, Tamara V., Safonova, Tatyana N., Tikhonov, Alexey V., Popov, Alexandre N., Popov, Vladimir O.

“…The structures of complexes of octahaem cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens (TvNiR) with the substrate sulfite…”
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Covalent modifications of the catalytic tyrosine in octahaem cytochrome c nitrite reductase and their effect on the enzyme activity by Trofimov, Anton A., Polyakov, Konstantin M., Tikhonova, Tamara V., Tikhonov, Alexey V., Safonova, Tatyana N., Boyko, Konstantin M., Dorovatovskii, Pavel V., Popov, Vladimir O.

“…Octahaem cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens (TvNiR), like the previously characterized pentahaem nitrite reductases (NrfAs),…”
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Correction: Trichlorobacter ammonificans, a dedicated acetate-dependent ammonifier with a novel module for dissimilatory nitrate reduction to ammonia by Sorokin, Dimitry Y, Tikhonova, Tamara V, Koch, Hanna, van den Berg, Eveline M, Hinderks, Renske S, Pabst, Martin, Dergousova, Natalia I, Solovevac, Anastasia Y, Kuenen, Gijs J, Popov, Vladimir O, van Loosdrecht, Mark C M, Lücker, Sebastian

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The O to S substitution in urea brings inhibition activity against thiocyanate dehydrogenase by Khrenova, Maria G., Soloveva, Anastasia Yu, Varfolomeeva, Larisa A., Tikhonova, Tamara V., Popov, Vladimir O.

“…[Display omitted] According to steady-state kinetic experiments, thiourea inhibits thiocyanate dehydrogenase TcDH, whereas urea does not. The QM/MM modeling…”
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Comparative Genomics of Thiohalobacter thiocyanaticus HRh1 T and Guyparkeria sp. SCN-R1, Halophilic Chemolithoautotrophic Sulfur-Oxidizing Gammaproteobacteria Capable of Using Thiocyanate as Energy Source by Tsallagov, Stanislav I, Sorokin, Dimitry Y, Tikhonova, Tamara V, Popov, Vladimir O, Muyzer, Gerard

“…The genomes of and (formerly known as ) sp. SCN-R1, two gammaproteobacterial halophilic sulfur-oxidizing bacteria (SOB) capable of thiocyanate oxidation via…”
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