1.8.99.5: dissimilatory sulfite reductase
This is an abbreviated version!
For detailed information about dissimilatory sulfite reductase, go to the full flat file.
Word Map on EC 1.8.99.5
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1.8.99.5
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sulfate-reducing
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desulfovibrio
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thiosulfate
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sulfur-oxidizing
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biogeochemical
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desulfobacteraceae
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geochemical
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vinosum
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desulfotomaculum
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allochromatium
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phylotypes
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adenosine-5'-phosphosulfate
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desulfoviridin
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desulfobulbus
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desulfosarcina
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hildenborough
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desulfobulbaceae
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chemotrophic
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desulfovibrionaceae
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low-sulfate
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sulfidogenic
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aarhus
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deltaproteobacterial
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chlorobaculum
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methane-oxidizing
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hydrogenotrophic
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desulfobacterium
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desulfomicrobium
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sirohaem
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desulfococcus
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t-rflp
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desulfosporosinus
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anme-2
- 1.8.99.5
-
sulfate-reducing
- desulfovibrio
- thiosulfate
-
sulfur-oxidizing
-
biogeochemical
- desulfobacteraceae
-
geochemical
- vinosum
- desulfotomaculum
- allochromatium
-
phylotypes
- adenosine-5'-phosphosulfate
-
desulfoviridin
- desulfobulbus
- desulfosarcina
- hildenborough
- desulfobulbaceae
-
chemotrophic
- desulfovibrionaceae
-
low-sulfate
-
sulfidogenic
-
aarhus
-
deltaproteobacterial
- chlorobaculum
-
methane-oxidizing
-
hydrogenotrophic
- desulfobacterium
- desulfomicrobium
-
sirohaem
- desulfococcus
-
t-rflp
- desulfosporosinus
-
anme-2
Reaction
+ 2 acceptor + 3 H2O = + + 2 reduced acceptor + 2 H+
Synonyms
CNL05500, dSiR, DsrA, DsrAB, DsrC, DsvA, DsvB, hydrogen-sulfide:(acceptor) oxidoreductase, MET5, octahaemcytochrome c MccA, PAE2566, SiRA, siroheme sulfite reductase, sulfite reductase
ECTree
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Metals Ions
Metals Ions on EC 1.8.99.5 - dissimilatory sulfite reductase
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Cu
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory hemecopper oxidases, the oxidation-labile Cu(I) centre of MccA does not seem to undergo a redox transition during catalysis. The copper-depleted form II of MccA, the absence of the heterometal allows for a binding mode of sulfite that is similar to the one seen in the siroheme-containing enzymes or in NrfA. In the structure of the Cu-containing, high-activity form I of MccA, all 12 monomers in the asymmetric unit have a ligand bound to heme 2
Fe
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A
Iron