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
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1.8.7.2
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thioredoxins
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chloroplast
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spinach
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redox-active
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reductases
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epr
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fe-s
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light-dependent
-
one-electron-reduced
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two-electron
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iron-sulfur
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raman
-
one-electron
-
variable-temperature
-
heterodisulfide
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dithiol
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methanosarcina
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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 + = 2 oxidized ferredoxin + + 2 H+
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
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Metals Ions
Metals Ions on EC 1.8.7.2 - ferredoxin:thioredoxin reductase
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Fe2+
Iron
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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
Fe2+
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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