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Literature summary extracted from

  • Jenner, L.P.; Kurth, J.M.; van Helmont, S.; Sokol, K.P.; Reisner, E.; Dahl, C.; Bradley, J.M.; Butt, J.N.; Cheesman, M.R.
    Heme ligation and redox chemistry in two bacterial thiosulfate dehydrogenase (TsdA) enzymes (2019), J. Biol. Chem., 294, 18002-18014 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.2.2 recombinant expression of Strep II-tagged enzyme Allochromatium vinosum
1.8.99.B2 recombinant expression of wild-type and mutant Strep II-tagged enzymes Campylobacter jejuni

Protein Variants

EC Number Protein Variants Comment Organism
1.8.2.2 C138H inactive Campylobacter jejuni
1.8.2.2 C138M inactive Campylobacter jejuni
1.8.2.2 N254K the enzyme shows 10fold reduced oxidation activity of thiosulfate but has a comparable maximum rate of tetrathionate reduction compared to the wild type enzyme Campylobacter jejuni
1.8.99.B2 C138H site-directed mutagenesis, spectroscopic and electrochemical mutant characterization Campylobacter jejuni
1.8.99.B2 C138M site-directed mutagenesis, spectroscopic and electrochemical mutant characterization Campylobacter jejuni
1.8.99.B2 N254K site-directed mutagenesis, spectroscopic and electrochemical mutant characterization Campylobacter jejuni

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.2.2 Fe2+ in the enzyme bound hemes Allochromatium vinosum
1.8.99.B2 Fe2+ in the enzyme bound hemes Campylobacter jejuni

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
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Campylobacter jejuni
-
 tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum DSM 180 cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum NCIMB 10441 cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum ATCC 17899 cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum NBRC 103801 cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum D cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
1.8.99.B2 tetrathionate + reduced electron acceptor Campylobacter jejuni
-
 2 thiosulfate + oxidized electron acceptor
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.8.2.2 Allochromatium vinosum
-
-
-
1.8.2.2 Allochromatium vinosum D3RVD4
-
-
1.8.2.2 Allochromatium vinosum ATCC 17899 D3RVD4
-
-
1.8.2.2 Allochromatium vinosum D D3RVD4
-
-
1.8.2.2 Allochromatium vinosum DSM 180 D3RVD4
-
-
1.8.2.2 Allochromatium vinosum NBRC 103801 D3RVD4
-
-
1.8.2.2 Allochromatium vinosum NCIMB 10441 D3RVD4
-
-
1.8.2.2 Campylobacter jejuni
-
-
-
1.8.99.B2 Campylobacter jejuni
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.2.2 2 thiosulfate + 2 ferricyanide
-
 Campylobacter jejuni tetrathionate + 2 ferrocyanide
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricyanide highest activity Allochromatium vinosum tetrathionate + 2 ferrocyanide
-
 ?
1.8.2.2 2 thiosulfate + 2 ferricytochrome c
-
 Allochromatium vinosum tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c
-
 Campylobacter jejuni tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c Allochromatium vinosum tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum DSM 180 tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c Allochromatium vinosum DSM 180 tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum NCIMB 10441 tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c Allochromatium vinosum NCIMB 10441 tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum ATCC 17899 tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c Allochromatium vinosum ATCC 17899 tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum NBRC 103801 tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c Allochromatium vinosum NBRC 103801 tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum D tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 2 thiosulfate + 2 ferricytochrome c for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c Allochromatium vinosum D tetrathionate + 2 ferrocytochrome c
-
 r
1.8.2.2 additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum ?
-
-
1.8.2.2 additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum DSM 180 ?
-
-
1.8.2.2 additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum NCIMB 10441 ?
-
-
1.8.2.2 additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum ATCC 17899 ?
-
-
1.8.2.2 additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum NBRC 103801 ?
-
-
1.8.2.2 additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum D ?
-
-
1.8.2.2 tetrathionate + reduced methyl viologen highest activity Campylobacter jejuni 2 thiosulfate + methyl viologen
-
 ?
1.8.2.2 tetrathionate + reduced methyl viologen very low activity Allochromatium vinosum 2 thiosulfate + methyl viologen
-
 ?
1.8.99.B2 additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Campylobacter jejuni ?
-
-
1.8.99.B2 tetrathionate + reduced electron acceptor
-
 Campylobacter jejuni 2 thiosulfate + oxidized electron acceptor
-
 r
1.8.99.B2 tetrathionate + reduced electron acceptor for CjTsdA the maximum rate of tetrathionate reduction is approximately twice that of thiosulfate oxidation Campylobacter jejuni 2 thiosulfate + oxidized electron acceptor
-
 r

Subunits

EC Number Subunits Comment Organism
1.8.2.2 ? x * 28142, calculated from amino acid sequence Allochromatium vinosum
1.8.2.2 ? x * 28142, mature protein with two c-hemes, without signal peptide, followed by a C-terminal extension of one additional amino acid and the Strep II-tag, sequence calculation Allochromatium vinosum
1.8.2.2 ? x * 37103, calculated from amino acid sequence Campylobacter jejuni
1.8.99.B2 ? x * 37103, mature protein with two c-hemes, without the signal peptide, and with an N-terminal Strep II-tag preceded by three amino acids and followed by four amino acids, sequence calculation Campylobacter jejuni

Synonyms

EC Number Synonyms Comment Organism
1.8.2.2 AvTsdA
-
 Allochromatium vinosum
1.8.2.2 di-heme TsdA
-
 Allochromatium vinosum
1.8.2.2 tetrathionate reductase
-
 Campylobacter jejuni
1.8.2.2 thiosulfate dehydrogenase
-
 Allochromatium vinosum
1.8.2.2 thiosulfate oxidase
-
 Allochromatium vinosum
1.8.2.2 TsdA
-
 Allochromatium vinosum
1.8.2.2 TsdA
-
 Campylobacter jejuni
1.8.99.B2 CjTsdA
-
 Campylobacter jejuni
1.8.99.B2 di-heme TsdA
-
 Campylobacter jejuni
1.8.99.B2 thiosulfate dehydrogenase
-
 Campylobacter jejuni
1.8.99.B2 TsdA
-
 Campylobacter jejuni

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.2.2 cytochrome c
-
 Allochromatium vinosum
1.8.2.2 cytochrome c
-
 Campylobacter jejuni
1.8.2.2 heme
-
 Allochromatium vinosum
1.8.2.2 heme
-
 Campylobacter jejuni
1.8.2.2 heme two heme c, heme 1 and heme 2, di-Fe(III), rapid interheme electron transfer determined from the AvTsdA crystal structure. Distal ligation of AvTsdA heme 2 is provided by Lys208 and Met209 Allochromatium vinosum
1.8.99.B2 heme two hemes, heme 1 and heme 2. Distal ligation of CjTsdA Heme 2 is provided by Asn254 and Met255 Campylobacter jejuni

General Information

EC Number General Information Comment Organism
1.8.2.2 physiological function thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states In Allochromatium vinosum TsdA, heme 2 reduction triggers a switch from His/Lys ligation to His/Met, but the rates of interconversion are such that His/Lys ligation is retained during turnover. Thiosulfate oxidation by enzyme AvTsdA provides electrons for photosynthesis Allochromatium vinosum
1.8.99.B2 physiological function thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states. In Campylobacter jejuni, TsdA heme 2 has His/Met ligation. Enzyme CjTsdA allows use of tetrathionate as a terminal respiratory electron sink Campylobacter jejuni