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Literature summary for 1.8.7.2 extracted from

  • Hirasawa, M.; Droux, M.; Gray, K.A.; Boyer, J.M.; Davis, D.J.; Buchanan, B.B.; Knaff, D.B.
    Ferredoxin-thioredoxin reductase: properties of its complex with ferredoxin. III (1988), Biochim. Biophys. Acta, 935, 1-8.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7
-
reduced ferredoxin native ferredoxin, pH 7.9 Spinacia oleracea
1.8
-
reduced ferredoxin ferredoxin modified by treatment with glycine ethyl ester in the presence of 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide, pH 7.9 Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid
-
Spinacia oleracea 9579
-

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Spinacia oleracea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced ferredoxin + thioredoxin disulfide
-
Spinacia oleracea 2 oxidized ferredoxin + thioredoxin + 2 H+
-
?
reduced ferredoxin + thioredoxin disulfide
-
Spinacia oleracea oxidized ferredoxin + thioredoxin + H+
-
r

Cofactor

Cofactor Comment Organism Structure
Ferredoxin ferredoxin-thioredoxin reductase forms an electrostatically stabilized 1:1 complex with ferredoxin. Chemical modification of three or four carboxyl groups on ferredoxin has little effect on its interaction with ferredoxin-thioredoxin reductase. The ferredoxin domain that binds ferredoxin-thioredoxin reductase is not completely identical to that involved in binding other ferredoxin-dependent enzymes Spinacia oleracea