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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

Reaction

2 thiosulfate +

2 ferricytochrome c
=
tetrathionate
+ 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

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.2 With a cytochrome as acceptor
                1.8.2.2 thiosulfate dehydrogenase

Crystallization

Crystallization on EC 1.8.2.2 - thiosulfate dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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