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Literature summary for 1.8.2.2 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
Search for more literature for 1.8.2.2

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of Strep II-tagged enzyme Allochromatium vinosum

Protein Variants

Protein Variants Comment Organism
C138H inactive Campylobacter jejuni
C138M inactive Campylobacter jejuni
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

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in the enzyme bound hemes Allochromatium vinosum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum
-
 tetrathionate + 2 ferrocytochrome c
-
 r
2 thiosulfate + 2 ferricytochrome c Campylobacter jejuni
-
 tetrathionate + 2 ferrocytochrome c
-
 r
2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum DSM 180 cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum NCIMB 10441 cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum ATCC 17899 cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum NBRC 103801 cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r
2 thiosulfate + 2 ferricytochrome c Allochromatium vinosum D cofactor with a heme c tetrathionate + 2 ferrocytochrome c
-
 r

Organism

Organism UniProt Comment Textmining
Allochromatium vinosum
-
-
-
Allochromatium vinosum D3RVD4
-
-
Allochromatium vinosum ATCC 17899 D3RVD4
-
-
Allochromatium vinosum D D3RVD4
-
-
Allochromatium vinosum DSM 180 D3RVD4
-
-
Allochromatium vinosum NBRC 103801 D3RVD4
-
-
Allochromatium vinosum NCIMB 10441 D3RVD4
-
-
Campylobacter jejuni
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 thiosulfate + 2 ferricyanide
-
 Campylobacter jejuni tetrathionate + 2 ferrocyanide
-
 ?
2 thiosulfate + 2 ferricyanide highest activity Allochromatium vinosum tetrathionate + 2 ferrocyanide
-
 ?
2 thiosulfate + 2 ferricytochrome c
-
 Allochromatium vinosum tetrathionate + 2 ferrocytochrome c
-
 r
2 thiosulfate + 2 ferricytochrome c
-
 Campylobacter jejuni tetrathionate + 2 ferrocytochrome c
-
 r
2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum tetrathionate + 2 ferrocytochrome c
-
 r
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
2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum DSM 180 tetrathionate + 2 ferrocytochrome c
-
 r
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
2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum NCIMB 10441 tetrathionate + 2 ferrocytochrome c
-
 r
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
2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum ATCC 17899 tetrathionate + 2 ferrocytochrome c
-
 r
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
2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum NBRC 103801 tetrathionate + 2 ferrocytochrome c
-
 r
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
2 thiosulfate + 2 ferricytochrome c cofactor with a heme c Allochromatium vinosum D tetrathionate + 2 ferrocytochrome c
-
 r
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
additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum ?
-
-
additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum DSM 180 ?
-
-
additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum NCIMB 10441 ?
-
-
additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum ATCC 17899 ?
-
-
additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum NBRC 103801 ?
-
-
additional information the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively Allochromatium vinosum D ?
-
-
tetrathionate + reduced methyl viologen highest activity Campylobacter jejuni 2 thiosulfate + methyl viologen
-
 ?
tetrathionate + reduced methyl viologen very low activity Allochromatium vinosum 2 thiosulfate + methyl viologen
-
 ?

Subunits

Subunits Comment Organism
? x * 28142, calculated from amino acid sequence Allochromatium vinosum
? 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
? x * 37103, calculated from amino acid sequence Campylobacter jejuni

Synonyms

Synonyms Comment Organism
AvTsdA
-
 Allochromatium vinosum
di-heme TsdA
-
 Allochromatium vinosum
tetrathionate reductase
-
 Campylobacter jejuni
thiosulfate dehydrogenase
-
 Allochromatium vinosum
thiosulfate oxidase
-
 Allochromatium vinosum
TsdA
-
 Allochromatium vinosum
TsdA
-
 Campylobacter jejuni

Cofactor

Cofactor Comment Organism Structure
cytochrome c
-
 Allochromatium vinosum
cytochrome c
-
 Campylobacter jejuni
heme
-
 Allochromatium vinosum
heme
-
 Campylobacter jejuni
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

General Information

General Information Comment Organism
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