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Literature summary for 1.8.7.2 extracted from

  • Staples, C.R.; Ameyibor, E.; Fu, W.; Gardet-Salvi, L.; Stritt-Etter, A.-L.; Schuermann, P.; Knaff, D.B.; Johnson, M.K.
    The nature and properties of the iron-sulfur center in spinach ferredoxin:thioredoxin reductase: A new biological role for iron-sulfur clusters (1996), Biochemistry, 35, 11425-11434.
    View publication on PubMed
Search for more literature for 1.8.7.2

Protein Variants

Protein Variants Comment Organism
additional information labeling of cysteinyl residues in the active site by alkylation and spectroscopic analysis, overview Spinacia oleracea

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ nature, properties, and function of the Fe-S cluster in spinach FTR, overview. [4Fe-4S]2+ cluster covalently attached through a cluster sulfide to a cysteine-based thiyl radical formed on one of the active-site thiols, and at least partial cluster oxidation to the [4Fe-4S]3+ state. Proposed canonical structures for the Fe-S cluster in N-ethylmaleimide-modified spinach FTR, overview. Detailed spectroscopic analysis Spinacia oleracea
Iron presence of an S = 0 [4Fe-4S]2+ cluster with complete cysteinyl-S coordination that cannot be reduced at potentials down to -650 mV, but can be oxidized by ferricyanide to an S = 1/2 [4Fe-4S]3+ state. The midpoint potential for the [4Fe-4S]3+/2+ couple is estimated to be +420 mV versus NHE. Results argue against a role for the cluster in mediating electron transport from ferredoxin to the active-site disulfide and suggest an alternative role for the cluster in stabilizing the one-electron-reduced intermediate. A mechanistic scheme is proposed involving sequential one-electron redox processes with the role of the [4Fe-4S]2+ cluster being to stabilize the thiyl radical formed by the initial one-electron reduction of the active-site disulfide Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from leaves Spinacia oleracea

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Spinacia oleracea
-

Synonyms

Synonyms Comment Organism
FTR
-
 Spinacia oleracea

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center presence of an S = 0 [4Fe-4S]2+ cluster with complete cysteinyl-S coordination that cannot be reduced at potentials down to -650 mV, but can be oxidized by ferricyanide to an S = 1/2 [4Fe-4S]3+ state. The midpoint potential for the [4Fe-4S]3+/2+ couple is estimated to be +420 mV versus NHE. Results argue against a role for the cluster in mediating electron transport from ferredoxin to the active-site disulfide and suggest an alternative role for the cluster in stabilizing the one-electron-reduced intermediate. A mechanistic scheme is proposed involving sequential one-electron redox processes with the role of the [4Fe-4S]2+ cluster being to stabilize the thiyl radical formed by the initial one-electron reduction of the active-site disulfide Spinacia oleracea

General Information

General Information Comment Organism
additional information role for Fe-S clusters in the enzyme mechanism involving both the stabilization of a thiyl radical intermediate and cluster site-specific chemistry involving a bridging sulfide Spinacia oleracea