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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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.2.2 gene tsdA, DNA and amino acid sequence analysis and sequence comparisons, the tsdA gene is immediately preceded by tsdB encoding for another diheme cytochrome Allochromatium vinosum
1.8.2.2 gene tsdA, DNA and amino acid sequence analysis and sequence comparisons, the tsdA gene is immediately preceded by tsdB encoding for another diheme cytochrome Marichromatium purpuratum

Protein Variants

EC Number Protein Variants Comment Organism
1.8.2.2 additional information construction of a fusion enzyme of Allochromatium vinosum TsdA and Marichromatium purpuratum TsdBA that reacts efficiently in vitro with high potential iron-sulfur protein from Allochromatium vinosum. High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains Marichromatium purpuratum
1.8.2.2 additional information construction of a fusion enzyme of Allochromatium vinosum TsdA and Marichromatium purpuratum TsdBA that reacts efficiently in vitro with high potential iron-sulfur protein from Allochromatium vinosum. High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains. Redox activity of AvTsdA adsorbed on a mesoporous nanocrystalline SnO2 electrode Allochromatium vinosum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.2.2 Fe2+ ferric hemes Allochromatium vinosum
1.8.2.2 Fe2+ ferric hemes Marichromatium purpuratum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum
-
 tetrathionate + 2 ferrocytochrome c
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Marichromatium purpuratum
-
 tetrathionate + 2 ferrocytochrome c
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum DSM 180
-
 tetrathionate + 2 ferrocytochrome c
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Marichromatium purpuratum 984
-
 tetrathionate + 2 ferrocytochrome c
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.2.2 Allochromatium vinosum D3RVD4
-
-
1.8.2.2 Allochromatium vinosum DSM 180 D3RVD4
-
-
1.8.2.2 Marichromatium purpuratum W0DW89
-
-
1.8.2.2 Marichromatium purpuratum 984 W0DW89
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.2.2 2 thiosulfate + 2 ferricytochrome c
-
 Allochromatium vinosum tetrathionate + 2 ferrocytochrome c
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricytochrome c
-
 Marichromatium purpuratum tetrathionate + 2 ferrocytochrome c
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricytochrome c
-
 Allochromatium vinosum DSM 180 tetrathionate + 2 ferrocytochrome c
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricytochrome c
-
 Marichromatium purpuratum 984 tetrathionate + 2 ferrocytochrome c
-
 ?
1.8.2.2 additional information thiosulfate is covalently bound to Cys330 on heme 3 of TsdA. Di-heme cytochrome TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism Marichromatium purpuratum ?
-
 ?
1.8.2.2 additional information thiosulfate is covalently bound to Cys330 on heme 3 of TsdA. Di-heme cytochrome TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism Marichromatium purpuratum 984 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.2.2 AvTsdA
-
 Allochromatium vinosum
1.8.2.2 diheme cytochrome c TsdA
-
 Allochromatium vinosum
1.8.2.2 diheme cytochrome c TsdA
-
 Marichromatium purpuratum
1.8.2.2 MpTsdBA
-
 Marichromatium purpuratum
1.8.2.2 TsdA
-
 Allochromatium vinosum
1.8.2.2 TsdA
-
 Marichromatium purpuratum

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.2.2 cytochrome c diheme cytochrome c TsdA, Allochromatium vinosum does not contain a second diheme cytochrome TsdB. Structure modelling, overview Allochromatium vinosum
1.8.2.2 cytochrome c diheme cytochrome c TsdB acts as an effective electron acceptor of TsdA in vitro when TsdA and TsdB originate from the same source organism. TsdAB tetraheme cytochrome c in the oxidized state 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. TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism. The four hemes are covalently bound to the polypeptide chain through thioether bonds formed by cysteine residues Cys21 and Cys24 for heme 1, Cys121 and Cys124 for heme 2, Cys287and Cys290 for heme 3, and Cys402 and Cys405 for heme 4, three hemes (hemes 1, 2, and 4) with His/Met coordination. Heme 3 exhibits axial ligation by His291, and the Sgamma atom of Cys330 is located in close vicinity to the heme iron such that it serves as the sixth ligand. Heme structure modelling, overview Marichromatium purpuratum

General Information

EC Number General Information Comment Organism
1.8.2.2 evolution the enzyme belongs to the thiosulfate dehydrogenase (TsdA) family. Axial ligation by histidine and cysteine is typical for the active site of TsdA proteins Allochromatium vinosum
1.8.2.2 evolution the enzyme belongs to the thiosulfate dehydrogenase (TsdA) family. Axial ligation by histidine and cysteine is typical for the active site of TsdA proteins Marichromatium purpuratum