EC Number ![](./images/down.png) ![](./images/up.png) |
Substrates ![](./images/down.png) ![](./images/up.png) |
Organism ![](./images/down.png) ![](./images/up.png) |
Products ![](./images/down.png) ![](./images/up.png) |
Reversibility ![](./images/down.png) ![](./images/up.png) |
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1.6.1.4 | more |
flavoenzyme, additionally shows NADPH-cytochrome c reductase activity, EC 1.6.2.4 |
Nitrobacter winogradskyi |
? |
- |
? |
1.6.1.4 | NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster |
in the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+). In the absence of ferredoxin, NAD+ is only very slowly reduced (less than 1% of the rate observed in the presence of ferredoxin) |
Clostridium kluyveri |
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster |
- |
r |
1.6.1.4 | NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster |
in the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+). In the absence of ferredoxin, NAD+ is only very slowly reduced (less than 1% of the rate observed in the presence of ferredoxin) |
Clostridium kluyveri DSM 555 |
NADH + H+ + 2 NADP+ + reduced ferredoxin iron-sulfur cluster |
- |
r |
1.6.1.4 | NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster |
reduction of both NAD+ and Fd by Nfn enzymes is coupled to the bifurcation of electrons from NADPH oxidation. The exergonic coupling of the NADP(H) and NAD(H) half reactions in Nfn is presumed to be mediated by NADPH oxidation at L-FAD followed by electron transfer to the proximal [2Fe-2S] cluster and subsequently the NAD(H) binding site at S-FAD. Biophysical analysis of the enzyme provides the first direct insight into the mechanism of flavin-based electron bifurcation and the requisite structural features |
Pyrococcus furiosus |
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster |
- |
? |
1.6.1.4 | NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster |
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH |
Clostridium kluyveri |
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster |
- |
r |
1.6.1.4 | NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster |
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH |
Clostridium kluyveri DSM 555 |
NAD+ + 2 NADPH + 2 reduced ferredoxin iron-sulfur cluster |
- |
r |
1.6.1.4 | NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster |
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH. In the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+) |
Clostridium kluyveri |
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster |
- |
r |
1.6.1.4 | NADH + H+ + 2 NADP+ + 2 reduced ferredoxin iron-sulfur cluster |
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH. In the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+) |
Clostridium kluyveri DSM 555 |
NAD+ + 2 NADPH + 2 oxidized ferredoxin iron-sulfur cluster |
- |
r |
1.6.1.4 | NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster |
- |
Pyrococcus furiosus |
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster |
- |
? |
1.6.1.4 | NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster |
- |
Nitrobacter winogradskyi |
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster |
0.064 mol of NAD + is reduced per mol of enzyme per s with NADPH produced continuously by glucose-6-phosphate dehydrogenase system |
? |