Unusual Cytochrome c 552 from Thioalkalivibrio paradoxus : Solution NMR Structure and Interaction with Thiocyanate Dehydrogenase.

Autor: Britikov, Vladimir V.¹ (AUTHOR), Bocharov, Eduard V.^2,3 (AUTHOR) edvbon@mail.ru, Britikova, Elena V.¹ (AUTHOR), Dergousova, Natalia I.⁴ (AUTHOR), Kulikova, Olga G.⁴ (AUTHOR), Solovieva, Anastasia Y.⁴ (AUTHOR), Shipkov, Nikolai S.⁴ (AUTHOR), Varfolomeeva, Larisa A.⁴ (AUTHOR), Tikhonova, Tamara V.⁴ (AUTHOR), Timofeev, Vladimir I.^2,5 (AUTHOR), Shtykova, Eleonora V.⁵ (AUTHOR), Altukhov, Dmitry A.⁶ (AUTHOR), Usanov, Sergey A.¹ (AUTHOR), Arseniev, Alexander S.² (AUTHOR), Rakitina, Tatiana V.² (AUTHOR), Popov, Vladimir O.⁴ (AUTHOR)

Publikováno v: International Journal of Molecular Sciences. Sep2022, Vol. 23 Issue 17, p9969. 25p.

Unusual Cytochrome c552 from Thioalkalivibrio paradoxus: Solution NMR Structure and Interaction with Thiocyanate Dehydrogenase

Autor: Vladimir V. Britikov, Eduard V. Bocharov, Elena V. Britikova, Natalia I. Dergousova, Olga G. Kulikova, Anastasia Y. Solovieva, Nikolai S. Shipkov, Larisa A. Varfolomeeva, Tamara V. Tikhonova, Vladimir I. Timofeev, Eleonora V. Shtykova, Dmitry A. Altukhov, Sergey A. Usanov, Alexander S. Arseniev, Tatiana V. Rakitina, Vladimir O. Popov

Publikováno v: International Journal of Molecular Sciences, Vol 23, Iss 17, p 9969 (2022)

The search of a putative physiological electron acceptor for thiocyanate dehydrogenase (TcDH) newly discovered in the thiocyanate-oxidizing bacteria Thioalkalivibrio paradoxus revealed an unusually large, single-heme cytochrome c (CytC552), which was

Externí odkaz: https://doaj.org/article/92fc435c03cf4dc5b2e1937cdccc14d3

Catalytic Properties of Flavocytochrome c Sulfide Dehydrogenase from Haloalkaliphilic Bacterium Thioalkalivibrio paradoxus

Autor: Evgenii M Osipov, Olga G Kulikova, Tamara V. Tikhonova, Anastasiya V Lilina, Nataliya I Dergousova, Vladimir Popov, Nikolay S Shipkov

Publikováno v: Biochemistry. Biokhimiia. 86(3)

Flavocytochrome c sulfide dehydrogenase (FCC) is one of the central enzymes of the respiratory chain in sulfur-oxidizing bacteria. FCC catalyzes oxidation of sulfide and polysulfide ions to elemental sulfur accompanied by electron transfer to cytochr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::679c4856ae7ff9b3d7066b0d4b9196f5
https://pubmed.ncbi.nlm.nih.gov/33838635

Характеристика каталитических свойств флавоцитохром с сульфиддегидрогеназы из галоалкалофильной бактерии Thioalkalivibrio paradoxus

Publikováno v: Биохимия. 86:422-430

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bfa9d4ba77efca009d4164050b58b8f5
https://doi.org/10.31857/s0320972521030106

Structure of the flavocytochrome C sulfide dehydrogenase associated with the copper-binding protein CopC from the haloalkaliphilic sulfuroxidizing bacterium thioalkalivibrio paradoxus ArH 1

Autor: Stanislav I. Tsallagov, Eugeny M. Osipov, Dimitry Y. Sorokin, Anastasia V. Lilina, Tamara V. Tikhonova, Vladimir Popov, T. N. Safonova

Publikováno v: Acta Crystallographica Section D: Structural Biology, 74(7)

Flavocytochrome c sulfide dehydrogenase from Thioalkalivibrio paradoxus (TpFCC) is a heterodimeric protein consisting of flavin- and monohaem c-binding subunits. TpFCC was co-purified and co-crystallized with the dimeric copper-binding protein TpCopC

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c5ba6079daf106df5e712cf954b0f23
https://doi.org/10.1107/s2059798318005648