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Literature summary for 1.18.1.2 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)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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]

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

Localization

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

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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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

Source Tissue Comment Organism Textmining
leaf isozyme L-FNR I 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
additional information the enzyme also shows NADPH-dependent cyt c reductase activity Zea mays ?
-
?

Synonyms

Synonyms Comment Organism
Fd-NADP+ reductase
-
Zea mays
FNR
-
Zea mays

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
Zea mays

General Information

General Information Comment Organism
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
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