EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
  1.19.1.1 | 2 ferricyanide + NADPH |
- |
Escherichia coli |
2 ferrocyanide + NADP+ + H+ |
- |
? |
| 1.19.1.1 | 2 ferricytochrome c2 + NADPH |
- |
Escherichia coli |
2 ferrocytochrome c2 + NADP+ + H+ |
- |
? |
| 1.19.1.1 | FMNH2 + NADP+ |
- |
Escherichia coli |
FMN + NADPH + H+ |
- |
? |
| 1.19.1.1 | more |
the enzyme reduces flavodoxin I, flavodoxin II and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner, i.e. reaction of EC 1.18.2.1. Flavodoxin I and flavodoxin II behave similarly with respect to FNR, with affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin. Flavodoxin I and flavodoxin II can obtain electrons from reduced Fd at rates that are comparable to those obtained with reduced FNR |
Escherichia coli |
? |
- |
? |
| 1.19.1.1 | more |
substrate flavodoxin is more structured when the FMN cofactor is bound. Holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase, whereas there is no detectable interaction between apo-flavodoxin and the protein |
Escherichia coli |
? |
- |
? |
| 1.19.1.1 | more |
the electron-transfer route is NADPH to FLDR to flavodoxin. The midpoint reduction potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples of FLDR are 2308 mV and 2268 mV, respectively. Binding of 2'-adenosine monophosphate increases the midpoint reduction potentials for both FLDR couples |
Escherichia coli |
? |
- |
? |
| 1.19.1.1 | oxidized cytochrome c + NADH + H+ |
- |
Escherichia coli |
reduced cytochrome c + NAD+ |
- |
r |
| 1.19.1.1 | oxidized cytochrome c + NADPH + H+ |
- |
Escherichia coli |
reduced cytochrome c + NADP+ |
- |
r |
| 1.19.1.1 | reduced 2,6-dichlorophenolindophenol + NADP+ |
- |
Escherichia coli |
oxidized 2,6-dichlorophenolindophenol + NADPH + H+ |
- |
? |
| 1.19.1.1 | reduced flavodoxin + NADP+ |
- |
Escherichia coli |
oxidized flavodoxin + NADPH + H+ |
- |
? |
