1.8.7.2: ferredoxin:thioredoxin reductase
This is an abbreviated version!
For detailed information about ferredoxin:thioredoxin reductase, go to the full flat file.
Word Map on EC 1.8.7.2
-
1.8.7.2
-
thioredoxins
-
chloroplast
-
spinach
-
redox-active
-
reductases
-
epr
-
fe-s
-
light-dependent
-
one-electron-reduced
-
two-electron
-
iron-sulfur
-
raman
-
one-electron
-
variable-temperature
-
heterodisulfide
-
dithiol
-
methanosarcina
-
synthesis
- 1.8.7.2
- thioredoxins
- chloroplast
- spinach
-
redox-active
- reductases
- epr
- fe-s
-
light-dependent
-
one-electron-reduced
-
two-electron
-
iron-sulfur
-
raman
-
one-electron
-
variable-temperature
-
heterodisulfide
- dithiol
-
methanosarcina
- synthesis
Reaction
2 reduced ferredoxin
+
Synonyms
Fd-thioredoxin reductase, Fd:TRX reductase, FdR, Fdx flavin-thioredoxin reductase, Fdx-dependent thioredoxin reductase, FDX-dependent TRX reductase, ferredoxin disulfide reductase, ferredoxin-dependent thioredoxin reductase, ferredoxin-thioredoxin reductase, FFTR, FTR, FTRc, glr0719, GvDTR, iron-sulfur ferredoxin-dependent thioredoxin reductase, Ma_1659, protein modulase
ECTree
1.8.7.2 ferredoxin:thioredoxin reductaseAdvanced search results
results (
results (Cofactor
Cofactor on EC 1.8.7.2 - ferredoxin:thioredoxin reductase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
FAD
in each monomer, two conserved Rossmann-type modules form the FAD-binding. The pi-stacking interaction between the side chain of the conserved tryptophan at the C-terminal tail of a monomer and the isoalloxazine ring of the FAD of an adjacent monomer at its re-face. This interaction seems to protect the flavin from the solvent, a distinctive feature of the GvDTR enzyme not found in other flavin thioredoxin reductases. The C-terminal extension stabilizes the semiquinone state of the flavin
4Fe-4S-center
-
midpoint potential value of + 340 mV. The midpoint potential value shifts slightly, to + 380 mV, in the N-ethylmaleimide-treated enzyme
4Fe-4S-center
-
presence of a unique iron site in the [4Fe-4S] cluster. Site-specific cluster chemistry, involving the formation of a five-coordinate Fe site with two cysteinate ligands, occurs during catalytic cycling of FTR
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
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
4Fe-4S-center
residues Cys52, Cys71, Cys73, and Cys82 bind the Fe-S cluster
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
-
Ferredoxin
Fdx, iron-sulfur ferredoxin, enzyme-Fdx interaction analysis, overview. Investigation of GvDTR and GvFdx1 or GvFdx2 as functional redox partners by analyzing the reduction of photosynthetic m-type thioredoxin (Trxm) in a mixture containing NADPH, the redox pair Anabaena ferredoxin-NADP+ reductase (AnFNR)/GvFdx1 or AnFNR/GvFdx2, GvDTR, and Gloeobacter Trx-m (GvTrxm). The redox state of GvTrx-m is examined with the thiol-specific reagent 4-acetamido-40-maleimidyldistilbene-2,2'-disulfonic acid (AMS), separating the reduced and oxidized proteins with nonreducing SDS-PAG.Only GvFdx1 with the complete reactants significantly increases the reduced/oxidized ratio of GvTrx-m, prompting the conclusion that GvFFTR interacts with GvFdx1 but not with GvFdx2, which has a unique C-terminal extension. GvFdx1 is a functional electron-delivering partner for GvDTR. GvFdx1 binding to GvDTR is strictly dependent on the presence of the enzyme's C-terminal tail. GvFdx1 (petF, gvip492) and GvFdx2 (gvip440) are recombinantly expressed as N-terminally His8-tagged proteins, with a TEV cleavage site preceding the Fdx sequence, in Escherichia coli Rosetta (DE3) pLys cells
-
