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Literature summary extracted from

  • Kurth, J.M.; Brito, J.A.; Reuter, J.; Flegler, A.; Koch, T.; Franke, T.; Klein, E.M.; Rowe, S.F.; Butt, J.N.; Denkmann, K.; Pereira, I.A.; Archer, M.; Dahl, C.
    Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase (2016), J. Biol. Chem., 291, 24804-24818.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.2.2 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 Allochromatium vinosum
1.8.2.5 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

EC Number Organism UniProt Comment Textmining
1.8.2.2 Allochromatium vinosum D3RVD4
-
-
1.8.2.5 Marichromatium purpuratum W0DW89
-
-
1.8.2.5 Marichromatium purpuratum 984 W0DW89
-
-

Synonyms

EC Number Synonyms Comment Organism
1.8.2.2 TsdA
-
 Allochromatium vinosum
1.8.2.5 MARPU_02550
-
 Marichromatium purpuratum
1.8.2.5 TsdA
-
 Marichromatium purpuratum

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.2.2 heme reduction of His/Cys-ligated heme 1 occurs reversibly between approximately -100 and -350 mV. Reduction of His/Lys-ligated heme 2 is proposed to occur between approximately +150 and -100 mV Allochromatium vinosum