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Literature summary for 1.18.1.2 extracted from

  • Dumit, V.I.; Essigke, T.; Cortez, N.; Ullmann, G.M.
    Mechanistic insights into ferredoxin-NADP(H) reductase catalysis involving the conserved glutamate in the active site (2010), J. Mol. Biol., 397, 814-825.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in the iron-sulfur center of ferredoxin Zea mays

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Zea mays
-
-
-

Reaction

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin + NADP+
-
Zea mays 2 oxidized ferredoxin + NADPH + H+
-
r

Synonyms

Synonyms Comment Organism
ferredoxin-NADP(H) reductase
-
Zea mays
FNR
-
Zea mays

Cofactor

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

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