1.13.11.55: sulfur oxygenase/reductase
This is an abbreviated version!
For detailed information about sulfur oxygenase/reductase, go to the full flat file.
Word Map on EC 1.13.11.55
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1.13.11.55
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ambivalens
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thiosulfate
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acidianus
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thermoacidophilic
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hollow
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non-heme
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disproportionation
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acidithiobacillus
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acidophil
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sulfobacillus
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tetrathionate
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tokodaii
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heterodisulfide
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bioleaching
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degradation
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low-potential
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caldus
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pharmacology
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industry
- 1.13.11.55
- ambivalens
- thiosulfate
- acidianus
-
thermoacidophilic
-
hollow
-
non-heme
-
disproportionation
- acidithiobacillus
-
acidophil
- sulfobacillus
- tetrathionate
- tokodaii
-
heterodisulfide
-
bioleaching
- degradation
-
low-potential
- caldus
- pharmacology
- industry
Reaction
4 sulfur + 4 H2O + = 2 hydrogen sulfide + 2 sulfite
Synonyms
AaSOR, SAMN00768000_1627, SAMN00768000_1798, SOR, SOR protein, SOR-AT, sulfur oxygenase, sulfur oxygenase reductase, sulfuroxygenasereductase, sulphur oxygenase reductase, TpSOR, TPY_0405
ECTree
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Crystallization
Crystallization on EC 1.13.11.55 - sulfur oxygenase/reductase
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X-ray crystallography of SOR wild-type crystals soaked with inhibitors Hg2+ and iodoacetamide, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, crystal structure analysis
structure at 1.73 A resolution. At the catalytic center, iron is ligated to His86, His90, Glu114, and two water molecules. Three conserved cysteines in the cavity are located 9.5-13 A from the iron and are observed as free thiol forms. The iron and Cys31 are essential
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