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Literature summary extracted from

  • Cherney, M.; Zhang, Y.; James, M.; Weiner, J.
    Structure-activity characterization of sulfide:quinone oxidoreductase variants (2012), J. Struct. Biol., 178, 319-328.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.5.4 expression in Escherichia coli Acidithiobacillus ferrooxidans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.5.4 crystal structures of the wild-type enzyme in complex with sodium selenide and gold(I) cyanide. Mechanism for the reduction of sulfides to elemental sulfur may involve nucleophilic attack of Cys356 on C4A atom of FAD or alternatively, an alternative anionic radical mechanism by direct electron transfer from Cys356 to the isoalloxazine ring of FAD Acidithiobacillus ferrooxidans

Protein Variants

EC Number Protein Variants Comment Organism
1.8.5.4 C128A about 35% of wild-type activity in assay with decylubiquinone Acidithiobacillus ferrooxidans
1.8.5.4 C128S loss of activity in assay with decylubiquinone Acidithiobacillus ferrooxidans
1.8.5.4 C160A loss of activity in assay with decylubiquinone, about 35% of wild-type activity for reduction of FAD fluorescence by Na2S Acidithiobacillus ferrooxidans
1.8.5.4 C356S loss of activity in assay with decylubiquinone, loss of activity for reduction of FAD fluorescence by Na2S Acidithiobacillus ferrooxidans
1.8.5.4 H132A about 40% of wild-type activity in assay with decylubiquinone Acidithiobacillus ferrooxidans
1.8.5.4 H198A about 60% of wild-type activity in assay with decylubiquinone Acidithiobacillus ferrooxidans
1.8.5.4 S126A about 35% of wild-type activity in assay with decylubiquinone Acidithiobacillus ferrooxidans

Organism

EC Number Organism UniProt Comment Textmining
1.8.5.4 Acidithiobacillus ferrooxidans B7JBP8
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1.8.5.4 Acidithiobacillus ferrooxidans DSM 14882 B7JBP8
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