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Literature summary for 1.8.7.2 extracted from

  • Staples, C.R.; Gaymard, E.; Stritt-Etter, A.L.; Telser, J.; Hoffman, B.M.; Schurmann, P.; Knaff, D.B.; Johnson, M.K.
    Role of the [Fe4S4] cluster in mediating disulfide reduction in spinach ferredoxin:thioredoxin reductase (1998), Biochemistry, 37, 4612-4620.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
N-ethylmaleimide spinach ferredoxin:thioredoxin reductase reduced with stoichiometric amounts of reduced benzyl viologen or frozen under turnover conditions in the presence of thioredoxin exhibits a slowly relaxing S = 1/2 resonance identical to that of a modified form of the enzyme in which one of the cysteines of the active-site disulfide is alkylated with N-ethylmaleimide. N-ethylmaleimide-TR is a stable analogue of a one-electron-reduced enzymatic intermediate Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Spinacia oleracea 9507
-

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.
additional information the catalytic mechanism involves S-based cluster chemistry to facilitate electron transfer to the active-site disulfide resulting in covalent attachment of the electron-transfer cysteine and generation of the free interchange cysteine that is required for the thiol-disulfide interchange reaction with thioredoxin Spinacia oleracea ?
-
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Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center presence of a [Fe4S4]3+ cluster that is coordinated by five cysteinates with little unpaired spin density delocalized onto the cluster-associated cysteine of the active-site disulfide. While the ligation site of the fifth cysteine remains undefined, the best candidate is a cluster bridging sulfide Spinacia oleracea