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Literature summary extracted from

  • Medina, M.; Gomez-Moreno, C.
    Interaction of ferredoxin-NADP+ reductase with its substrates: optimal interaction for efficient electron transfer (2004), Photosynth. Res., 79, 113-131.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.18.1.2
-
 Spinacia oleracea

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.2 E139K site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 E301A site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 K138E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 K290E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 K294E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 K72E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 K75E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 L76D site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 L76F site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 L76S site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 L76V site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 L78D site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 L78F site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 L78S site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 L78V site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 R100A site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 R16E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
1.18.1.2 R264E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.18.1.2 chloroplast associated to the grana fraction Spinacia oleracea 9507
-
1.18.1.2 membrane weakly bound Spinacia oleracea 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 reduced ferredoxin + NADP+ Anabaena sp. delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Spinacia oleracea delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis, enzyme-substrate interactions, overview oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Escherichia coli reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Azotobacter vinelandii reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism, removal of free radicals gegnerated during the metabolsim oxidized ferredoxin + NADPH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Anabaena sp.
-
-
-
1.18.1.2 Azotobacter vinelandii
-
-
-
1.18.1.2 Escherichia coli
-
-
-
1.18.1.2 Spinacia oleracea
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism via semiquinone intermediate and radical formation Escherichia coli
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism via semiquinone intermediate and radical formation Azotobacter vinelandii
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism via semiquinone intermediate and radical formation, enzyme-substrate interactions, overview Spinacia oleracea
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism via semiquinone intermediate and radical formation, enzyme-substrate interactions, overview Anabaena sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 additional information the enzyme is asscoiated to phycobilin pigments Anabaena sp. ?
-
 ?
1.18.1.2 reduced ferredoxin + NADP+ delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis Anabaena sp. oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis, enzyme-substrate interactions, overview Spinacia oleracea oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism Escherichia coli oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism, removal of free radicals gegnerated during the metabolsim Azotobacter vinelandii oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ plant-type ferredoxin contains a [2Fe2S] cluster, enzyme requires ferredoxin, substrate is a bulky protein, enzyme-substrate interactions involve residues R16, K72, K88, K116, E139, R264, K290, and K294, overview Spinacia oleracea oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ plant-type ferredoxin contains a [2Fe2S] cluster, substrate is an acidic, bulky protein, enzyme-substrate interactions involve residues R16, K72, K75, R100, E139, R264, K290, and K294 Anabaena sp. oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ substrate is a bulky protein Escherichia coli oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ substrate is a bulky protein Azotobacter vinelandii oxidized ferredoxin + NADPH
-
 r

Subunits

EC Number Subunits Comment Organism
1.18.1.2 More three-dimensional structure analysis, intramolecular stabilization and stabilizationof enzyme-substrate complex, overview Anabaena sp.
1.18.1.2 More three-dimensional structure analysis, overview Escherichia coli
1.18.1.2 More three-dimensional structure analysis, overview Spinacia oleracea
1.18.1.2 More three-dimensional structure analysis, overview Azotobacter vinelandii

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 FNR
-
 Escherichia coli
1.18.1.2 FNR
-
 Spinacia oleracea
1.18.1.2 FNR
-
 Azotobacter vinelandii
1.18.1.2 FNR
-
 Anabaena sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions Escherichia coli
1.18.1.2 FAD involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions Spinacia oleracea
1.18.1.2 FAD involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions Azotobacter vinelandii
1.18.1.2 FAD involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions Anabaena sp.
1.18.1.2 NADP+
-
 Escherichia coli
1.18.1.2 NADP+
-
 Azotobacter vinelandii
1.18.1.2 NADP+ interaction with the enzyme, complex structure, specificity-determining structures, overview Spinacia oleracea
1.18.1.2 NADP+ interaction with the enzyme, complex structure, specificity-determining structures, overview Anabaena sp.