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
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General Information
General Information on EC 1.8.2.6 - S-disulfanyl-L-cysteine oxidoreductase
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physiological function
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overview on structure and function of the soxXYZABCD gene cluster and comparison with other organisms. The Sox system reconstituted from SoxXA, SoxYZ, SoxB, and SoxCD mediates thiosulfate-, sulfite-, sulfur-, and hydrogen sulfide-dependent cytochrome c reduction. SoxCD acts as a dehydrogenase at a protein-bound sulfur atom
physiological function
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recombinant SoxX, SoxY, SoxZ, SoxA, SoxB, and SoxCD protein mixture degrades H2S in dose- and time-dependent manners. All recombinant Sox enzymes are necessary for degrading H2S
physiological function
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the sulfur-oxidizing enzyme system reconstituted from proteins SoxXA, SoxYZ, SoxB, and SoxCD releases 8 mol of electrons per mol of thiosulfate. Omission of SoxCD from the system reduces the rate of thiosulfate oxidation by 70% and the electron yield to 2 mol of electrons per mol of thiosulfate. SoxCD is also required for the maximum rates of hydrogen sulfide-, sulfur-, and sulfite-dependent cytochrome c reduction, which are 18, 25, and 60% of the rate with SoxCD included, respectively
physiological function
-
the sulfur-oxidizing enzyme system reconstituted from proteins SoxXA, SoxYZ, SoxB, and SoxCD releases 8 mol of electrons per mol of thiosulfate. Omission of SoxCD from the system reduces the rate of thiosulfate oxidation by 70% and the electron yield to 2 mol of electrons per mol of thiosulfate. SoxCD is also required for the maximum rates of hydrogen sulfide-, sulfur-, and sulfite-dependent cytochrome c reduction, which are 18, 25, and 60% of the rate with SoxCD included, respectively
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physiological function
-
recombinant SoxX, SoxY, SoxZ, SoxA, SoxB, and SoxCD protein mixture degrades H2S in dose- and time-dependent manners. All recombinant Sox enzymes are necessary for degrading H2S
-