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Literature summary for 1.18.1.2 extracted from

  • Nogues, I.; Perez-Dorado, I.; Frago, S.; Bittel, C.; Mayhew, S.G.; Gomez-Moreno, C.; Hermoso, J.A.; Medina, M.; Cortez, N.; Carrillo, N.
    The ferredoxin-NADP(H) reductase from Rhodobacter capsulatus: molecular structure and catalytic mechanism (2005), Biochemistry, 44, 11730-11740.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH hydride exchange occurs at 30-150 per s being not limiting for enzyme activity. Electron transfer to flavodoxin proceeds at 2.7 per s, in the range of steady-state catalysis, supporting that flavodoxin oscillates between the semiquinone and fully reduced states when enzyme operates in vivo Rhodobacter capsulatus
a

Cofactor

Cofactor Comment Organism Structure
FAD structure contains two domains harboring FAD and NAD(P)H binding sites Rhodobacter capsulatus
NADH structure contains two domains harboring FAD and NAD(P)H binding sites Rhodobacter capsulatus
NADPH structure contains two domains harboring FAD and NAD(P)H binding sites Rhodobacter capsulatus