1.8.2.6: S-disulfanyl-L-cysteine oxidoreductase
This is an abbreviated version!
For detailed information about S-disulfanyl-L-cysteine oxidoreductase, go to the full flat file.
Word Map on EC 1.8.2.6
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1.8.2.6
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sulfur-oxidizing
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pantotrophus
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paracoccus
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thiosulfate
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chemotrophic
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soxxa
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sulfane
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dissimilatory
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chemolithoautotrophic
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molybdopterin
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flavocytochrome
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allochromatium
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thioalkalivibrio
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heme-1
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haloalkaliphilic
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vinosum
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six-electron
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medicine
- 1.8.2.6
-
sulfur-oxidizing
- pantotrophus
-
paracoccus
- thiosulfate
-
chemotrophic
- soxxa
-
sulfane
-
dissimilatory
-
chemolithoautotrophic
- molybdopterin
-
flavocytochrome
-
allochromatium
- thioalkalivibrio
-
heme-1
-
haloalkaliphilic
- vinosum
-
six-electron
- medicine
Reaction
+ 6 ferricytochrome c + 3 H2O = + 6 ferrocytochrome c + 6 H+
Synonyms
Daro_3133, Daro_3134, SoxCD, sulfite-dehydrogenase, sulfur dehydrogenase
ECTree
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Cofactor
Cofactor on EC 1.8.2.6 - S-disulfanyl-L-cysteine oxidoreductase
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cytochrome c
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the cytochrome c motifs of subunit SoxD are buried in the protein core
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subunit SoxD harbors two heme domains. 3.65 mol of heme per mol of enzyme tetramer. Exclusively the heme-1 domain of SoxD is required for activity, substrate specificity, and electron yield of the sulfur-oxidizing system
heme
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the side chains of His297, Arg316 and the main chain nitrogen atoms of Ser327 and Lys360 are involved in H-bonding with the oxygen atoms of the heme propionate group