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Literature summary for 1.8.2.5 extracted from
- Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase (2016), J. Biol. Chem., 291, 24804-24818.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 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 | Marichromatium purpuratum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Marichromatium purpuratum | W0DW89 | - |
- |
| Marichromatium purpuratum 984 | W0DW89 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MARPU_02550 | - |
Marichromatium purpuratum |
| TsdA | - |
Marichromatium purpuratum |
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Release 2023.1 (January 2023)
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