ferredoxin-NADP+ reductase | |||||||||
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Identifiers | |||||||||
EC number | 1.18.1.2 | ||||||||
CAS number | 9029-33-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Search | |
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PMC | articles |
PubMed | articles |
NCBI | proteins |
In enzymology, a ferredoxin-NADP+ reductase (EC 1.18.1.2) abbreviated FNR, is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are reduced ferredoxin, NADP+, and H+, whereas its two products are oxidized ferredoxin and NADPH. It has a flavin cofactor, FAD.
This enzyme belongs to the family of oxidoreductases, that use iron-sulfur proteins as electron donors and NAD+ or NADP+ as electron acceptors.
This enzyme participates in photosynthesis.
The systematic name of this enzyme class is ferredoxin:NADP+ oxidoreductase. Other names in common use include:
During photosynthesis, electrons are removed from water and transferred to the single electron carrier ferredoxin. Ferredoxin: NADP+ reductase then transfers an electron from each of two ferredoxin molecules to a single molecule of the two electron carrier NADPH. FNR utilizes FAD, which can exist in an oxidized state, single electron reduced semiquinone state, and fully reduced state to mediate this electron transfer.