This membrane-bound bacterial enzyme catalyses the direct oxidation of sulfite to sulfate in the cytoplasm. The enzyme, characterized from the bacteria Ruegeria pomeroyi and Allochromatium vinosum, is a complex that consists of a membrane anchor (SoeC) and two cytoplasmic subunits: an iron-sulfur protein (SoeB) and a molybdoprotein that contains a [4Fe-4S] iron-sulfur cluster (SoeA). cf. EC 1.8.2.1, sulfite dehydrogenase (cytochrome).
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SYSTEMATIC NAME
IUBMB Comments
sulfite:quinone oxidoreductase
This membrane-bound bacterial enzyme catalyses the direct oxidation of sulfite to sulfate in the cytoplasm. The enzyme, characterized from the bacteria Ruegeria pomeroyi and Allochromatium vinosum, is a complex that consists of a membrane anchor (SoeC) and two cytoplasmic subunits: an iron-sulfur protein (SoeB) and a molybdoprotein that contains a [4Fe-4S] iron-sulfur cluster (SoeA). cf. EC 1.8.2.1, sulfite dehydrogenase (cytochrome).
the enzyme catalyzes sulfite oxidation using Nitro-blue tetrazolium as artificial electron acceptor at pH 7.8 and 60°C. The enzyme specifically oxidizes sulfite but can work in the reverse direction, reduction of sulfur or tetrathionate, using reduced methyl viologen (MV) as electron donor, thiosulfate is not able to act as an electron acceptor from MV, absence of reduction of thiosulfate by SoeABC. Oxidation of sodium tetrathionate by SoeABC is performed using DCPIP (2,6-dichlorophenolindophenol) in the presence or absence of phenazine methosulfate (PMS). No oxidation of sulfite, tetrathionate, polysulfide or thiosulfate, SoeABC seems therefore to oxidize sulfite specifically
the enzyme catalyzes sulfite oxidation using Nitro-blue tetrazolium as artificial electron acceptor at pH 7.8 and 60°C. The enzyme specifically oxidizes sulfite but can work in the reverse direction, reduction of sulfur or tetrathionate, using reduced methyl viologen (MV) as electron donor, thiosulfate is not able to act as an electron acceptor from MV, absence of reduction of thiosulfate by SoeABC. Oxidation of sodium tetrathionate by SoeABC is performed using DCPIP (2,6-dichlorophenolindophenol) in the presence or absence of phenazine methosulfate (PMS). No oxidation of sulfite, tetrathionate, polysulfide or thiosulfate, SoeABC seems therefore to oxidize sulfite specifically
enzyme Soe contains, in its active site, a molybdenum atom coordinated by two molecules of pyranopterin guanosine dinucleotide (therefore also named Mo-bisPGD enzymes) rather than a single pyranopterin
required, enzyme Soe contains, in its active site, a molybdenum atom coordinated by two molecules of pyranopterin guanosine dinucleotide (therefore also named Mo-bisPGD enzymes) rather than a single pyranopterin
the enzyme is membrane-bound and quinone reactive (via the SoeC subunit), facing the cytoplasm where SoeB (a module that carries FeeS centers) and the SoeA (the Mo-carrying catalytic subunit) are exposed. The enzyme is a large membrane-bound complex, formerly called SreABC
a mutant in which the region between genes CT0868 and CT0876 is replaced by a transposon insertion resulting in the truncation or deletion of nine genes including a quinone-interacting membrane-bound oxidoreductase (Qmo) complex (CT0866-0868), hypothetical proteins (CT0869-0875) and sulfide:quinone oxidoreductase is completely defective for growth on thiosulfate as the sole electron donor, but only slightly defective for growth on sulfide or thiosulfate plus sulfide. The strain does not oxidize thiosulfate and also displayes a defect in acetate assimilation under all growth conditions
SoeABC is the major sulfite-oxidizing enzyme in Allochromatium vinosum. The periplasmic sulfur substrate-binding protein SoxYZ is needed in parallel to the cytoplasmic enzymes for effective sulfite oxidation. A SoeABC-deficient mutant displays about 17% of wild-type sulifte oxidation. A knockout of both adenosine-5'-phosphosulfate reductase gene aprB and soeA leads to an additive effect with a residual specific rate of sulfite oxidation for whole cells of only 7%
SoeABC is the major sulfite-oxidizing enzyme in Allochromatium vinosum. The periplasmic sulfur substrate-binding protein SoxYZ is needed in parallel to the cytoplasmic enzymes for effective sulfite oxidation. A SoeABC-deficient mutant displays about 17% of wild-type sulifte oxidation. A knockout of both adenosine-5'-phosphosulfate reductase gene aprB and soeA leads to an additive effect with a residual specific rate of sulfite oxidation for whole cells of only 7%
a mutant in which the region between genes CT0868 and CT0876 is replaced by a transposon insertion resulting in the truncation or deletion of nine genes including a quinone-interacting membrane-bound oxidoreductase (Qmo) complex (CT0866-0868), hypothetical proteins (CT0869-0875) and sulfide:quinone oxidoreductase is completely defective for growth on thiosulfate as the sole electron donor, but only slightly defective for growth on sulfide or thiosulfate plus sulfide. The strain does not oxidize thiosulfate and also displayes a defect in acetate assimilation under all growth conditions
x * 108950, molybdoprotein SoeA carrying one [Fe4S4] cluster at the N-terminus, x * 26995, iron-sulfur protein SoeB, predicted to bind four [Fe4S4] clusters, and x * 35715, NrfD/PsrC-like membrane protein SoeC with eight transmembrane helices
x * 108950, molybdoprotein SoeA carrying one [Fe4S4] cluster at the N-terminus, x * 26995, iron-sulfur protein SoeB, predicted to bind four [Fe4S4] clusters, and x * 35715, NrfD/PsrC-like membrane protein SoeC with eight transmembrane helices
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 23fold from cell membranes via solubilization by various non-ionic detergents, centrifugation at 40000 x g, followed by anion exchange chromatography, ultrafiltration, and gel filtration
transcription of all SoeABC genes is about 3fold increased during photolithoautotrophic growth on sulfide or thiosulfate compared to photo organoheterotrophic growth on malate
transcription of all SoeABC genes is about 3fold increased during photolithoautotrophic growth on sulfide or thiosulfate compared to photo organoheterotrophic growth on malate
transcription of all SoeABC genes is about 3fold increased during photolithoautotrophic growth on sulfide or thiosulfate compared to photo organoheterotrophic growth on malate
Dahl, C.; Franz, B.; Hensen, D.; Kesselheim, A.; Zigann, R.
Sulfite oxidation in the purple sulfur bacterium Allochromatium vinosum: Identification of SoeABC as a major player and relevance of SoxYZ in the process
Microbiology
159
2626-2638
2013
Allochromatium vinosum (D3RNN8 and D3RNN7 and D3RNN6), Allochromatium vinosum, Allochromatium vinosum DSM 180 (D3RNN8 and D3RNN7 and D3RNN6)