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

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

1 Oxidoreductases

1.8 Acting on a sulfur group of donors

1.8.7 With an iron-sulfur protein as acceptor

1.8.7.2 ferredoxin:thioredoxin reductase

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Results	in table
3764	AA Sequence
1	Application
1	CAS Registry Number
7	Cloned(Commentary)
21	Cofactor
8	Crystallization (Commentary)
1	Expression
21	General Information
2	Inhibitors
2	KM Value [mM]
10	Localization
3	Metals/Ions
7	Molecular Weight [Da]
9	Natural Substrates/ Products (Substrates)
37	Organism
10	PDB ID
1	pH Optimum
2	pI Value
1	Posttranslational Modification
12	Protein Variants
5	Purification (Commentary)
3	Reaction
37	Reference
1	Renatured (Commentary)
14	Source Tissue
31	Substrates and Products (Substrate)
17	Subunits
34	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

Metals Ions

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Metals Ions on EC 1.8.7.2 - ferredoxin:thioredoxin reductase

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Fe2+

2 entries

Iron

Spinacia oleracea

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

702192