1.8.2.1: sulfite dehydrogenase (cytochrome)
This is an abbreviated version!
For detailed information about sulfite dehydrogenase (cytochrome), go to the full flat file.
Word Map on EC 1.8.2.1
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1.8.2.1
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starkeya
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novella
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thiosulfate
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paracoccus
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pantotrophus
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molybdoenzyme
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sulfoacetaldehyde
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desulfonation
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chemolithotrophic
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food industry
- 1.8.2.1
-
starkeya
- novella
- thiosulfate
-
paracoccus
- pantotrophus
-
molybdoenzyme
- sulfoacetaldehyde
-
desulfonation
-
chemolithotrophic
- food industry
Reaction
+ + = + 2 ferrocytochrome c + 2 H+
Synonyms
CT1015, dehydrogenase, sulfite, MccACD, Mo-dependent sulfite dehydrogenase, More, multiheme cytochrome c sulfite reductase, SDH, SiR-FP18, SiRA, SO, SOR, SorA, SorAB, SorT, SoxF, sulfate oxidase, sulfite cytochrome c reductase, sulfite dehydrogenase, sulfite oxidase, sulfite oxidoreductase, sulfite reductase, sulfite-cytochrome c oxidoreductase, sulfite-oxidizing molybdenum enzyme, sulfite-oxido-reductase, sulfite: ferricytochrome-c oxidoreductase, sulphite:cytochrome c oxidoreductase
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Metals Ions
Metals Ions on EC 1.8.2.1 - sulfite dehydrogenase (cytochrome)
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Iron
Mo
Mo4+
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molybdenum enzyme. Sulfite oxidizing enzymes (regardless of origin) share a common active site comprising a dioxido-MoVI moiety chelated by a molybdopterin dithiolene ligand in addition to a cysteinyl S-donor. The equatorial oxido ligand is the one transferred to sulfite during its 2-electron O-atom transfer reaction
Molybdenum
Iron
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Mo-based and Fe-based voltametric responses from the enzyme in the absence of substrate
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consists of a single molybdenum atom coordinated through the dithiolene group of a single molybdopterin molecule
Mo
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does not play a rate defining role in the catalytic mechanism of SDH before turnover
Mo
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Mo-PPT binding catalytic subunit (SorA) comprised of an SUOX fold and a dimerization domain
Molybdenum
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the 43897 Da subunit contains the 455 Da molybdenum cofactor, 1.3 mol of molybdenum per mol of enzyme
Molybdenum
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the 40600 Da subunit contains the molybdenum cofactor. Mo-based and Fe-based voltametric responses from the enzyme in the absence of substrate
Molybdenum
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The molybdenum atom of the oxidized enzyme is bound by two ModO ligands at 1.73 aangstroem and three thiolate ModS ligands at 2.42 aangstroem, whereas the reduced enzyme has one oxo at 1.74 aangstroem, one long oxygen at 2.19 aangstroem (characteristic of ModOH2), and three ModS ligands at 2.40 aangstroem