Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | in the iron-sulfur center of ferredoxin | Zea mays |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin + NADP+ | Zea mays | - |
2 oxidized ferredoxin + NADPH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH | FNR is able to transfer electrons between one-electron carriers, ferredoxin or flavodoxin, and two-electron carriers, NADP+ and NADPH, involving its redox cofactor FAD, involvement of Glu312 in the FNR catalytic mechanism not only as a proton donor but also as a key residue for stabilizing and destabilizing reaction intermediates, reaction mechanism and catalytic cycle, overview | Zea mays |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin + NADP+ | - |
Zea mays | 2 oxidized ferredoxin + NADPH + H+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
ferredoxin-NADP(H) reductase | - |
Zea mays |
FNR | - |
Zea mays |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | noncovalently bound, the flavin can adopt three different redox forms as the oxidized quinone form FAD, the one-electron reduced semiquinone radical form FADHradical, and the fully reduced quinol form FADH2 | Zea mays |
General Information | Comment | Organism |
---|---|---|
additional information | titration behaviour of Glu312, overview | Zea mays |
physiological function | in chloroplasts and cyanobacteria, FNR provides the NADPH necessary for photosynthetic CO2 assimilation | Zea mays |