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BRENDA support ferredoxin:CoB-CoM heterodisulfide reductase

This is an abbreviated version!
For detailed information about ferredoxin:CoB-CoM heterodisulfide reductase, go to the full flat file.


2 oxidized ferredoxin [iron-sulfur] cluster +

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= 2 reduced ferredoxin [iron-sulfur] cluster +
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+ 2 H+


CoB-CoM heterodisulfide reductase, CoB-CoM heterodisulfide reductase iron-sulfur subunit A, CoB-S-S-CoM reductase, Coenzyme B-Coenzyme M heterodisulfide reductase, ferredoxin:heterodisulfide oxidoreductase, HDR, hdrA1B1C1, hdrA2B2C2, HdrABC, HdrB, HdrB2, HdrB2C2, HdrD, heterodisulfide reductase, Mhun_1838, More


     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.7 With an iron-sulfur protein as acceptor
                EC ferredoxin:CoB-CoM heterodisulfide reductase


Purification on EC - ferredoxin:CoB-CoM heterodisulfide reductase

for references in articles please use BRENDA:EC1.8.7.3

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phenyl-Sepharose column chromatography, and Superdex 200 gel filtration
purification of a massive (megadalton) complex of the electron-bifurcating Fdh-Hdr together with the CO2-reducing Fmd (Fdh-Hdr-Fmd hexamer), as well as of dimeric Fdh-Hdr-Fmd and Fdh-Hdr subcomplexes by anion exchange chromatography and gel filtration. Mass spectrometry reveals that the Fdh-Hdr-Fmd complex elutes from gel filtration primarily as a 1-MDa dimer of subunits FdhAB-MvhD-HdrABCFmdABCDFG. The Fdh-Hdr complexes are isolated as two oligomeric states, which contain FdhAB-MvhD-HdrABCFmdF. Two of five isoenzymes of FdhA and are detected in all complexes
Q-Sepharose column chromatography and Superdex 200 gel filtration