1.8.2.2: thiosulfate dehydrogenase
This is an abbreviated version!
For detailed information about thiosulfate dehydrogenase, go to the full flat file.
Word Map on EC 1.8.2.2
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1.8.2.2
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sulfur
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sulfite
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thiobacillus
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rhodanese
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sulfur-oxidizing
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chemolithoautotrophic
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ferrooxidans
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vinosum
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allochromatium
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paracoccus
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acidithiobacillus
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thiooxidans
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tn5-mob
- 1.8.2.2
- sulfur
- sulfite
- thiobacillus
- rhodanese
-
sulfur-oxidizing
-
chemolithoautotrophic
- ferrooxidans
- vinosum
-
allochromatium
-
paracoccus
-
acidithiobacillus
- thiooxidans
-
tn5-mob
Reaction
2 thiosulfate + = + 2 ferrocytochrome c + 4 H+
Synonyms
AFE_0042, Alvin_0091, AvTsdA, C8J_0815, D0Y83_01395, di-heme TsdA, DIE28_04650, diheme cytochrome c TsdA, enzymes, thiosulfate-oxidizing, MpTsdBA, oxidase, thiosulfate, Tat pathway signal sequence domain protein, tetrathionate reductase, tetrathionate synthase, thiosulfate dehydrogenase, thiosulfate oxidase, thiosulfate-acceptor oxidoreductase, thiosulfate-oxidizing enzyme, TSD, TsdA
ECTree
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Crystallization
Crystallization on EC 1.8.2.2 - thiosulfate dehydrogenase
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purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.003 ml of 8 mg/ml protein in 20 mM Bis-Tris-HCl, pH 6.5, with 0.0015 ml of reservoir solution containing 23.5% w/v PEG 3350, 0.2 M (NH4)2SO4, 0.1 M Bis-Tris, pH 6.28, and 0.1 M NaI, and equilibration against 0.120 ml of reservoir solution, 20°C, method optimization, X-ray diffraction structure determination and analysis at 1.98 A resolution. The protein crystallized in space group C2 with one molecule in the asymmetric unit. Initial crystallization trials renders multiple, urchin-like crystals with no diffraction ability. Using iodide as an additive significantly improves the X-ray diffraction quality of the crystals
purified recombinant wild-type and K208N and K208G mutant enzymes, freeor in complex with tetrathionate, dithionite, or bisulfit, sitting drop vapour diffusion method, mixing of 0.003 ml of 8 mg/ml protein in 20 mM Bis-Tris-HCl, pH 6.5, with 0.0015 ml of reservoir solution containing 23.5% w/v PEG 3350, 0.2 M (NH4)2SO4, 0.1 M Bis-Tris, pH 6.28, and 0.1 M NaI, and equilibration against 0.120 ml of reservoir solution, the complex crystals are formed by soaking in an excess of ligands, tetrathionate, dithionite, and bisulfite, 20°C, X-ray diffraction structure determination and analysis at 1.40-1.98 A resolution, modelling
three-dimensional structure of the fusion protein with electron-transferring protein TsdB, to 2.75 A resolution. In the oxidized state, the tetraheme cytochrome c contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Thiosulfate is covalently bound to Cys330 on heme 3