Thiosulfate Dehydrogenase download

Thiosulfate Dehydrogenase Noelia Penelope Greer

Book Details:

Author: Noelia Penelope Greer
Published Date: 25 Dec 2011
Publisher: Patho Publishing
Original Languages: English
Book Format: Paperback::84 pages
ISBN10: 6139364272
ISBN13: 9786139364275
Publication City/Country: United States
Dimension: 152x 229x 5mm::136g

Download: Thiosulfate Dehydrogenase

Thiosulfate Dehydrogenase download . Abstract. The enzymes of the thiosulfate dehydrogenase (TsdA) family are wide-spread diheme c-type cytochromes.Here, redox carriers were studied mediating the flow of electrons arising from thiosulfate oxidation into respiratory or photosynthetic electron chains. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a cytochrome as acceptor. K16936 doxA; thiosulfate dehydrogenase [quinone] small subunit Enzymes [BR:ko01000] 1. Oxidoreductases 1.8 Acting on a sulfur group of donors 1.8.5 With a quinone or similar compound as acceptor 1.8.5.2 thiosulfate dehydrogenase (quinone) K16936 doxA; thiosulfate dehydrogenase [quinone] small subunit Abstract. Paracoccus pantotrophus strain GBsoxFΔ carries a deletion in the soxF gene that inactivates flavoprotein SoxF-sulfide dehydrogenase. This strain grew with thiosulfate slower than the wild type. GBsoxFΔ cells oxidized thiosulfate at a rate of 40% and hydrogen sulfide at a rate of 45% of the wild type.Complementation of GBsoxFΔ with plasmid pRIsoxF carrying the soxF gene increased FEBS Letters 350 (1994) 61-65 FEBS 14345 Sulfide dehydrogenase is identical with the SoxB protein of the thiosulfate-oxidizing enzyme system of Paracoccus denitrficans GB17 Angela Schneider, Cornelius Friedrich* Lehrstuhl fur Technische Mikrobiologie, Fachbereich Chemietechnik, Universitat Dortmund, D-44221 Dortmund, Germany. Characterization of a novel thiosulfate dehydrogenase from a marine acidophilic sulfur-oxidizing bacterium, Acidithiobacillus thiooxidans strain SH Sultana Sharmin, Eriko Yoshino, Tadayoshi Kanao and Kazuo Kamimura* Division of Agricultural and Life Science, Graduate School of Environmental and Life Science, Okayama University, Okayama, Japan Comments: The reaction can also proceed with ferricyanide as the electron acceptor, but more slowly. Unlike EC 1.8.2.2, thiosulfate dehydrogenase, this enzyme cannot utilize cytochrome c as an acceptor. Links to other databases To fill this gap, the gene coding for the thiosulfate dehydrogenase enzyme from Allochromatium vinosum was recombinantly expressed in Escherichia coli and its product purified, kinetic and spectroscopically characterized. Morevoer, we have determined its crystallographic structure in several redox states. Thiosulfate dehydrogenase (quinone). Alternative Name(s) Thiosulfate oxidoreductase, tetrathionate-forming. Thiosulfate:quinone oxidoreductase. TQO. Reaction catalysed; 2 thiosulfate + 6-decylubiquinone => tetrathionate + 6-decylubiquinol: Comment(s) The reaction can also proceed with ferricyanide as the electron acceptor, but more slowly. 1. Fukumori, Y. And Yamanaka, T. A high-potential nonheme iron protein (HiPIP)-linked, thiosulfate-oxidizing enzyme derived from Chromatium vinosum. Curr. Microbiol. 3 (1979) 117-120. 2. Lu, W.-P. And Kelly, D.P. Cellular location and partial purification of the 'thiosulphate-oxidizing enzyme' and several are known to contain heme prosthetic groups (e.g., thiosulfate dehydrogenase from T. Acidiphilus [2], sulfite reductase, and sulfite dehydrogenase [3]). The importance of these transformations in nature has lead us to investigate the reactions and electrochemistry of iron porphyrins in the presence of thiosulfate and sulfate. These Thiosulfate dehydrogenase activity was determined spectrophotometrically using ferricyanide as an artificial electron acceptor. The reaction was followed the thiosulfate-dependent decrease in ferricyanide absorbance at 420 nm. In enzymology, a thiosulfate dehydrogenase (quinone) (EC 1.8.5.2) is an enzyme that catalyzes the chemical reaction. 2 thiosulfate + 2 6-decylubiquinone ⇌ tetrathionate + 2 6-decylubiquinol. Thus, the two substrates of this enzyme are thiosulfate and 6-decylubiquinone, whereas its two products are tetrathionate and 6-decylubiquinol. This enzyme belongs to the family of oxidoreductases The relevant interconversion is not reversible at inert electrodes. However, facile reduction of S4O62– to S2O32– and the reverse reaction are catalyzed enzymes of the thiosulfate dehydrogenase, TsdA, family adsorbed on graphite electrodes. In this work, we performed a thorough structural and biochemical analysis of a purple bacterial thiosulfate dehydrogenase. The protein was found to contain two heme groups, both with unusual axial coordination. In the oxidized state, heme 1 has a His 53 /Cys 96 ligation, whereas heme 2 is coordinated His 164 /Lys 208. The reaction can also proceed with ferricyanide as the electron acceptor, but more slowly. Unlike EC 1.8.2.2, thiosulfate dehydrogenase, this enzyme cannot utilize cytochrome c as an acceptor. In this work we identified the gene for the tetrathionate-forming thiosulfate dehydrogenase (TsdA) from the purple sulfur bacterium Allochromatium vinosum sequence analysis and reverse genetics. The recombinant protein produced in Escherichia coli is a periplasmic, monomeric 25.8 kDa dihaem cytochrome c with an enzyme activity optimum at pH 4. anoxygenic sulfide and thiosulfate oxidation in photolithotrophic and facultative anaerobic chemolithotrophic bacteria, correlates with the lack of sulfur dehydrogenase (SoxCD), normally present in the thiosulfate-oxidizing multi-enzyme system (TOMES; Friedrich et al., 2005). The latter is a characteristic feature of microorganisms that Thiosulfate dehydrogenase is known to play a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans.Enzyme activity measured using ferricyanide as the electron acceptor was detected in cell extracts of A. Ferrooxidans ATCC 23270 grown on tetrathionate or sulfur, but no activity was detected in ferrous iron-grown cells. Partial purification of the crude preparation of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans. Approximately 20 mg of protein were applied on the column. Buffers: (A) 50 mM phosphate buffer, pH 7.0; (B) the same as (A) but with 2 M sodium chloride. In the purple sulfur bacterium Allochromatium vinosum, the reaction is catalyzed the periplasmic diheme c-type cytochrome thiosulfate dehydrogenase (TsdA). Here, we report the crystal structure of the "as isolated"form of A. Vinosum TsdA to 1.98 � resolution and those of several redox states of the enzyme to different resolutions. Thiosulfate induced cells of Paracoccus denitrificans GB17 oxidize thiosulfate and sulfide to sulfate. A mutant carrying a Tn5‐mob insertion in the soxB gene is unable to oxidize thiosulfate or sul tsdA (Thiosulfate dehydrogenase) FEATURES Loading DESCRIPTION. Loading EXTERNAL LINKS. Loading tsdA Thiosulfate dehydrogenase. Quick links: home MOLECULAR SYNOPSIS. Line_weight STRUCTURAL LIGANDABILITY. Panorama_fish_eye CANCER TYPES 2019. Jenner, L. P., Kurth, J. M., van Helmont, S., Sokol, K. P., Reisner, E., Dahl, C., Bradley, J. M., Butt, J. N. & Cheeseman, M. (2019) Heme ligation and redox Sulfide dehydrogenase is identical with the SoxB protein of the thiosulfate-oxibizing enzyme system of Paracoccus denitr@ans GB 17 Angela Schneider, Cornelius Friedrich* Lehrstuhl fiir Technische Mkrobiologie, Fachbereich Chemietechnik, Universitiit Dortmund, D-44221 Dortmund, Germany. Thiosulfate Dehydrogenase (TsdA) from Allochromatium vinosum: Structural and Functional Insights into Thiosulfate Oxidation Jos� A. Brito 1*,Kevin Denkmann 2*,In�s A. C. Pereira 1 Camelina sativa is an oil seed crop which can be grown on marginal lands. Camelina seed oil is rich in omega-3 fatty acids (>35%) and γ-tocopherol but is also high in erucic acid and glucosinolates. Camelina meal, is the -product after the oil has been extracted. Camelina meal was fed to 28 d old weaned pigs at 3.7% and 7.4% until age 56 d. Read "Thiosulfate dehydrogenase: a widespread unusual acidophilic c ‐type cytochrome, Environmental Microbiology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips. Sodium nitrite and sodium thiosulfate is a combination medicine that is used as an antidote to cyanide poisoning.Sodium nitrite and sodium thiosulfate works helping cells in the body convert cyanide to a form that can be removed from the body through urination. The enzyme catalyses the reversible formation of a sulfur-sulfur bond between the sulfane atoms of two thiosulfate molecules, yielding tetrathionate and releasing two electrons. In many bacterial species the enzyme is a diheme c -type cytochrome. Sodium thiosulfate (STS) is an industrial chemical which has also been approved for the treatment of certain rare medical conditions. These include cyanide poisoning and calciphylaxis in hemodialysis patients with end-stage kidney disease. Here, we investigated the anti-inflammatory activity of STS in our glial-mediated neuroinflammatory model. Thiosulfate dehydrogenase is known to play a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans. Enzyme activity measured using ferricyanide as the electron acceptor was detected in cell extracts of A. Ferrooxidans ATCC 23270 grown on tetrathionate or sulfur, but no activity was detected in ferrous iron-grown cells. The

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