Ligand [2Fe-2S]-center

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Basic Ligand Information

Molecular Structure
Picture of [2Fe-2S]-center (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C12H20Fe2N4O4R8S6
[2Fe-2S]-center
LGSDUERFIJETBW-HNWZVNCFSA-J
Synonyms:
oxidized [2Fe-2S] ferredoxin, reduced [2Fe-2S] ferredoxin

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (11 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
show the reaction diagram
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2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
show the reaction diagram
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S-adenosyl-L-methionine + adenine2503 in 23S rRNA + reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
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dethiobiotin + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
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protein N6-(octanoyl)lysine + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
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In Vivo Product in Enzyme-catalyzed Reactions (11 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
show the reaction diagram
-
-
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-
-
S-adenosyl-L-methionine + adenine2503 in 23S rRNA + reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-
-
dethiobiotin + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-
-
protein N6-(octanoyl)lysine + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (19 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-
S-adenosyl-L-methionine + adenine2503 in 23S rRNA + reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-
dethiobiotin + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-
protein N6-(octanoyl)lysine + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (19 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-
-
S-adenosyl-L-methionine + adenine2503 in 23S rRNA + reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-
-
dethiobiotin + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
-
-
protein N6-(octanoyl)lysine + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] ferredoxin
show the reaction diagram
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Enzyme Cofactor/Cosubstrate (72 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
ADH contains 5.9 Fe2+ and 2.06 acid-labile sulfurs per heterodimer
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HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters; HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters
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NdmA enzyme is a Rieske (2Fe-2S) non-heme iron monooxygenase that requires a partner reductase, NdmD, to transfer electrons from NADH
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sequence contains conserved amino acid motif -R-x12-CxHRxxxLxxG-x8-CxYHR-x6-G- for the Rieske [2Fe-2S] binding domain
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under ideal conditions, the hydroxylated product yield is about 50% of the diiron centers, suggesting that the enzyme operates by half-sites reactivity mechanisms
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reductase subunit CymAb
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the enzyme contains two [2Feľ2S] centers
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small subunit contains two [2Fe-2S] clusters
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the 31000 Da subunit contains one FAD (S-FAD) and a [2Fe-2S] cluster. The [2Fe-2S] cluster is unusual, with a relatively high (positive) reduction potential and coordination by one Asp and three Cys ligands
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presence of a planar [2Fe-2S] cluster in the N-terminal domain, where Fe1 is tetrahedrally coordinated by two bridging sulfide ions and two cysteines and Fe2 is three-coordinated by two bridging sulfides and one cysteine (Cys200)
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each monomer is composed of two domains in which the N-terminal domain forms a binding site for a [2Fe-2S] cluster and a Mg2+ ion
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DHAD can accommodate [Fe2S2] and [Fe4S4] clusters. Only the [Fe2S2] cluster-bound form is catalytically active. The [Fe2S2] cluster is coordinated by at least one non-cysteinyl ligand, which can be replaced by the thiol group(s) of dithiothreitol. [Fe2S2] cluster-containing NFU2 protein is likely the physiological cluster donor for in vivo maturation of DHAD
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; OsD27 contains a [2Fe-2S] iron-sulfur cluster that is required for catalysis
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complex contains one non-covalently bound FAD, one noncovalently bound riboflavin, ubiquinone-8 and a [2Feľ2S] cluster
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Metals and Ions (3 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
6.9 mol per mol of enzyme dimer, type I and type II [2Fe-2S]-centers
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the small subunit contains two [2Fe-2S] centers
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the [2Fe-2S] cluster in SdhB-N and center C in SdhC are two succinate reducible high-potential centers detected in the archaeal succinate:caldariellaquinone oxidoreductase complex that differ in their arrangements of the cluster-binding cysteine motifs and the local cluster surroundings. a biological [2Fe-2S] cluster breakdown under reducing conditions generally releases Fe2+ from the polypeptide chain into the aqueous solution, and the Fe2+ might then be recruited as a secondary ferrous iron source for de noVo biosynthesis and/or regulation of iron-binding enzymes in the cellular system
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Enzyme Kinetic Parameters

KM Value (1 result)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0014
-
at pH 6.8, temperature not specified in the publication

References & Links

Links to other databases for [2Fe-2S]-center

ChEBI
PubChem
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PubChem