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Literature summary extracted from

  • Kimata-Ariga, Y.; Sakakibara, Y.; Ikegami, T.; Hase, T.
    Electron transfer of site-specifically cross-linked complexes between ferredoxin and ferredoxin-NADP+ reductase (2010), Biochemistry, 49, 10013-10023.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.2 co-expression of wild-type and mutant ferredoxin and Fd-NADP+ reductases in Escherichia coli strain BL21(DE3) Zea mays

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.2 E19C site-directed mutagenesis of isozyme L-FNR I, NADPH-dependent cyt c reduction activity with different recombinant wild-type and mutant ferredoxins, in comparison to the wild-type enzyme, NMR chemical shift perturbation analysis, overview Zea mays
1.18.1.2 E25C site-directed mutagenesis of isozyme L-FNR I, NADPH-dependent cyt c reduction activity with different recombinant wild-type and mutant ferredoxins, in comparison to the wild-type enzyme, NMR chemical shift perturbation analysis, overview Zea mays
1.18.1.2 E36C site-directed mutagenesis of isozyme L-FNR I, NADPH-dependent cyt c reduction activity with different recombinant wild-type and mutant ferredoxins, in comparison to the wild-type enzyme, NMR chemical shift perturbation analysis, overview Zea mays
1.18.1.2 additional information introduction of specific disulfide bonds between ferredoxin and Fd-NADP+ reductase by engineering cysteines into the two proteins Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information stopped flow kinetic analysis Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.18.1.2 chloroplast
-
 Zea mays 9507
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 2 reduced ferredoxin + NADP+ Zea mays
-
 2 oxidized ferredoxin + NADPH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.2 recombinant wild-type and mutant ferredoxin and Fd-NADP+ reductases from Escherichia coli strain BL21(DE3) the latter as homodimers, separation to monomers and crosslinking, further purification of crosslinked complexes by anion exchange chromatography and gel filtration Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.18.1.2 leaf isozyme L-FNR I Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 2 reduced ferredoxin + NADP+
-
 Zea mays 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 additional information the enzyme also shows NADPH-dependent cyt c reductase activity Zea mays ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 Fd-NADP+ reductase
-
 Zea mays
1.18.1.2 FNR
-
 Zea mays

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.1.2 25
-
 assay at Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.1.2 7.5
-
 assay at Zea mays

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD
-
 Zea mays

General Information

EC Number General Information Comment Organism
1.18.1.2 additional information introduction of specific disulfide bonds between ferredoxin and Fd-NADP+ reductase by engineering cysteines into the two proteins results in 13 different Fd-FNR cross-linked complexes displaying a broad range of activity to catalyze the NADPH-dependent cytochrome c reduction Zea mays
1.18.1.2 physiological function ferredoxin and Fd-NADP+ reductase are redox partners responsible for the conversion between NADP+ and NADPH in the plastids of photosynthetic organisms Zea mays