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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

Reaction

[SoxY protein]-S-disulfanyl-L-cysteine
+ 6 ferricytochrome c + 3 H2O =
[SoxY protein]-S-sulfosulfanyl-L-cysteine
 + 6 ferrocytochrome c + 6 H+

Synonyms

Daro_3133, Daro_3134, SoxCD, sulfite-dehydrogenase, sulfur dehydrogenase

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.2 With a cytochrome as acceptor
                1.8.2.6 S-disulfanyl-L-cysteine oxidoreductase

Crystallization

Crystallization on EC 1.8.2.6 - S-disulfanyl-L-cysteine oxidoreductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular docking studies and comparison of the molecular mechanism of sulfur oxidation process in Dechloromonas aromatica and Thiobacillus denitrificans, the latter using proteins SoxAX instead of proteins SoxCD for recycling of SoxY. The SoxYZ protein of SoxCD lacking Thiobacillus denitrificans is more stable and interactive, in comparison with the SoxYZ complex from SoxCD-possessing Dechloromonas aromatica
Q47BB7; Q47BB8
crystal structure of SoxCD1, solved at 1.33 A . SoxCD1 misses the heme-2 domain D2 and is catalytically as active as SoxCD.The substrate of SoxCD is the outer (sulfane) sulfur of Cys-110-persulfide located at the C-terminal peptide swinging arm of SoxY of the SoxYZ carrier complex. The oxidation reactions of the sulfane-sulfur are initiated by the nucleophilic attack of the persulfide anion on the molybdenum atom that is, in turn, reduced. The close proximity of heme-1 to the molybdopterin allows easy acceptance of the electrons
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homology modeling of structure. SoxD belongs to the di-heme cytochrome c family of electron transport proteins whereas soxC gene product (SoxC) is a sulfur dehydrogenase
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