Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

a [DsrC protein]-S-sulfanyl-L-cysteine
+ 2 acceptor + 3 H2O =
sulfite
 +
a [DsrC protein]-dithiol
 + 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

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.99 With unknown physiological acceptors
                1.8.99.5 dissimilatory sulfite reductase

Metals Ions

Metals Ions on EC 1.8.99.5 - dissimilatory sulfite reductase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 heme–copper 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